{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T00:31:18Z","timestamp":1791592278248,"version":"4.3.4"},"reference-count":234,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2018,8,1]],"date-time":"2018-08-01T00:00:00Z","timestamp":1533081600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,3]],"date-time":"2020-09-03T00:00:00Z","timestamp":1599091200000},"content-version":"vor","delay-in-days":764,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100009619","name":"Japan Agency for Medical Research and Development","doi-asserted-by":"publisher","award":["JP18gm0910005j0004"],"award-info":[{"award-number":["JP18gm0910005j0004"]}],"id":[{"id":"10.13039\/100009619","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","award":["17H06417"],"award-info":[{"award-number":["17H06417"]}],"id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jlr.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Lipid Research"],"published-print":{"date-parts":[[2018,8]]},"DOI":"10.1194\/jlr.r085324","type":"journal-article","created":{"date-parts":[[2018,6,8]],"date-time":"2018-06-08T15:20:09Z","timestamp":1528471209000},"page":"1341-1366","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":84,"title":["Lipid transfer proteins rectify inter-organelle flux and accurately deliver lipids at membrane contact sites"],"prefix":"10.1016","volume":"59","author":[{"given":"Kentaro","family":"Hanada","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1194\/jlr.R085324_bib1","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1038\/nrm2330","article-title":"Membrane lipids: where they are and how they behave","volume":"9","author":"van Meer","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib2","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1038\/nature13474","article-title":"Lipid landscapes and pipelines in membrane homeostasis","volume":"510","author":"Holthuis","year":"2014","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib3","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/nrm.2017.138","article-title":"Understanding the diversity of membrane lipid composition","volume":"19","author":"Harayama","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/tra.12230","article-title":"Phospholipid synthesis and transport in mammalian cells","volume":"16","author":"Vance","year":"2015","journal-title":"Traffic."},{"key":"10.1194\/jlr.R085324_bib5","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/B978-0-444-63438-2.00007-9","article-title":"Phospholipid synthesis in mammalian cells","author":"Ridgway","year":"2016","journal-title":"Biochemistry of Lipids, Lipoproteins and Membranes."},{"key":"10.1194\/jlr.R085324_bib6","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1111\/tra.12193","article-title":"Interorganelle trafficking of lipids: preface for the thematic review series","volume":"15","author":"Hanada","year":"2014","journal-title":"Traffic."},{"key":"10.1194\/jlr.R085324_bib7","doi-asserted-by":"crossref","first-page":"2526","DOI":"10.1016\/j.bbamcr.2013.01.028","article-title":"Organization and function of membrane contact sites","volume":"1833","author":"Helle","year":"2013","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib8","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.tcb.2016.08.010","article-title":"Piecing together the patchwork of contact sites","volume":"27","author":"Gatta","year":"2017","journal-title":"Trends Cell Biol."},{"key":"10.1194\/jlr.R085324_bib9","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.plipres.2007.03.003","article-title":"Comparative genomics and evolution of eukaryotic phospholipid biosynthesis","volume":"46","author":"Lykidis","year":"2007","journal-title":"Prog. Lipid Res."},{"key":"10.1194\/jlr.R085324_bib10","doi-asserted-by":"crossref","first-page":"29808","DOI":"10.1074\/jbc.M005786200","article-title":"Cloning, genomic organization, and characterization of a human cholinephosphotransferase","volume":"275","author":"Henneberry","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib11","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.bbalip.2012.09.009","article-title":"Phosphatidylcholine and the CDP-choline cycle","volume":"1831","author":"Fagone","year":"2013","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib12","doi-asserted-by":"crossref","first-page":"3148","DOI":"10.1091\/mbc.01-11-0540","article-title":"The major sites of cellular phospholipid synthesis and molecular determinants of fatty acid and lipid head group specificity","volume":"13","author":"Henneberry","year":"2002","journal-title":"Mol. Biol. Cell."},{"key":"10.1194\/jlr.R085324_bib13","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1016\/j.cmet.2013.03.018","article-title":"Tam41 is a CDP-diacylglycerol synthase required for cardiolipin biosynthesis in mitochondria","volume":"17","author":"Tamura","year":"2013","journal-title":"Cell Metab."},{"key":"10.1194\/jlr.R085324_bib14","doi-asserted-by":"crossref","first-page":"E634","DOI":"10.3390\/ijms18030634","article-title":"Phosphoinositides, major actors in membrane trafficking and lipid signaling pathways","volume":"18","author":"De Craene","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1194\/jlr.R085324_bib15","doi-asserted-by":"crossref","DOI":"10.1002\/bies.201700121","article-title":"Phosphoinositide diversity, distribution, and effector function: stepping out of the box","volume":"39","author":"Choy","year":"2017","journal-title":"BioEssays."},{"key":"10.1194\/jlr.R085324_bib16","doi-asserted-by":"crossref","first-page":"24184","DOI":"10.1016\/S0021-9258(18)54410-0","article-title":"A Chinese hamster cDNA encoding a protein essential for phosphatidylserine synthase I activity","volume":"266","author":"Kuge","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib17","doi-asserted-by":"crossref","first-page":"17199","DOI":"10.1074\/jbc.273.27.17199","article-title":"Genetic evidence that phosphatidylserine synthase II catalyzes the conversion of phosphatidylethanolamine to phosphatidylserine in Chinese hamster ovary cells","volume":"273","author":"Saito","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib18","doi-asserted-by":"crossref","first-page":"6370","DOI":"10.1016\/S0021-9258(18)38127-4","article-title":"A cloned gene encoding phosphatidylserine decarboxylase complements the phosphatidylserine biosynthetic defect of a Chinese hamster ovary cell mutant","volume":"266","author":"Kuge","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib19","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1111\/tra.12239","article-title":"Sphingolipid metabolism and interorganellar transport: localization of sphingolipid enzymes and lipid transfer proteins","volume":"16","author":"Yamaji","year":"2015","journal-title":"Traffic."},{"key":"10.1194\/jlr.R085324_bib20","doi-asserted-by":"crossref","first-page":"6387","DOI":"10.1021\/cr2002917","article-title":"Sphingolipid and glycosphingolipid metabolic pathways in the era of sphingolipidomics","volume":"111","author":"Merrill","year":"2011","journal-title":"Chem. Rev."},{"key":"10.1194\/jlr.R085324_bib21","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1016\/j.bbalip.2013.06.006","article-title":"Co-evolution of sphingomyelin and the ceramide transport protein CERT","volume":"1841","author":"Hanada","year":"2014","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib22","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1038\/nrm2336","article-title":"Cellular cholesterol trafficking and compartmentalization","volume":"9","author":"Ikonen","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib23","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/B978-0-444-63438-2.00011-0","article-title":"Cholestrol synthesis","author":"Brown","year":"2016","journal-title":"Biochemistry of Lipids, Lipoproteins and Membranes"},{"key":"10.1194\/jlr.R085324_bib24","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1111\/tra.12177","article-title":"Binding domain-driven intracellular trafficking of sterols for synthesis of steroid hormones, bile acids and oxysterols","volume":"15","author":"Midzak","year":"2014","journal-title":"Traffic."},{"key":"10.1194\/jlr.R085324_bib25","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1126\/science.271.5255.1526","article-title":"Coat proteins and vesicle budding","volume":"271","author":"Schekman","year":"1996","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib26","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1126\/science.272.5259.227","article-title":"Protein sorting by transport vesicles","volume":"272","author":"Rothman","year":"1996","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib27","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1083\/jcb.101.2.441","article-title":"Intracellular transport of phosphatidylcholine to the plasma membrane","volume":"101","author":"Kaplan","year":"1985","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib28","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1083\/jcb.101.2.446","article-title":"Transport of cholesterol from the endoplasmic reticulum to the plasma membrane","volume":"101","author":"Kaplan","year":"1985","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib29","doi-asserted-by":"crossref","first-page":"24906","DOI":"10.1016\/S0021-9258(18)35849-6","article-title":"Sphingolipid transport in mitotic HeLa cells","volume":"267","author":"Collins","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib30","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/nrm.2015.8","article-title":"Structure and function of ER membrane contact sites with other organelles","volume":"17","author":"Phillips","year":"2016","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib31","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1016\/j.tcb.2016.05.007","article-title":"Stitching organelles: organization and function of specialized membrane contact sites in plants","volume":"26","author":"P\u00e9rez-Sancho","year":"2016","journal-title":"Trends Cell Biol."},{"key":"10.1194\/jlr.R085324_bib32","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1007\/BF00343816","article-title":"Submicroscopical structure of cytoplasmic basophils in the liver, pancreas and salivary gland; study of ultrafine slices by electron microscope","volume":"37","author":"Bernhard","year":"1952","journal-title":"Z. Zellforsch. Mikrosk. Anat."},{"key":"10.1194\/jlr.R085324_bib33","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1084\/jem.100.6.641","article-title":"Studies on the endoplasmic reticulum. I. Its identification in cells in situ","volume":"100","author":"Palade","year":"1954","journal-title":"J. Exp. Med."},{"key":"10.1194\/jlr.R085324_bib34","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1083\/jcb.144.6.1135","article-title":"Golgi structure in three dimensions: functional insights from the normal rat kidney cell","volume":"144","author":"Ladinsky","year":"1999","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib35","doi-asserted-by":"crossref","first-page":"7248","DOI":"10.1016\/S0021-9258(19)39106-9","article-title":"Phospholipid synthesis in a membrane fraction associated with mitochondria","volume":"265","author":"Vance","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib36","doi-asserted-by":"crossref","first-page":"3596","DOI":"10.1016\/S0021-9258(19)34182-1","article-title":"Exchange of phospholipids between liver mitochondria and microsomes in vitro","volume":"243","author":"Wirtz","year":"1968","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib37","doi-asserted-by":"crossref","first-page":"11501","DOI":"10.1073\/pnas.96.20.11501","article-title":"Mice without phosphatidylcholine transfer protein have no defects in the secretion of phosphatidylcholine into bile or into lung airspaces","volume":"96","author":"van Helvoort","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.R085324_bib38","doi-asserted-by":"crossref","first-page":"1828","DOI":"10.1126\/science.7892608","article-title":"Role of steroidogenic acute regulatory protein in adrenal and gonadal steroidogenesis","volume":"267","author":"Lin","year":"1995","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib39","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1056\/NEJM199612193352503","article-title":"International Congenital Lipoid Adrenal Hyperplasia Consortium. The pathophysiology and genetics of congenital lipoid adrenal hyperplasia","volume":"335","author":"Bose","year":"1996","journal-title":"N. Engl. J. Med."},{"key":"10.1194\/jlr.R085324_bib40","doi-asserted-by":"crossref","first-page":"26285","DOI":"10.1074\/jbc.273.41.26285","article-title":"Steroidogenic acute regulatory protein (StAR) is a sterol transfer protein","volume":"273","author":"Kallen","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib41","doi-asserted-by":"crossref","first-page":"106","DOI":"10.3389\/fendo.2016.00106","article-title":"Adrenal mitochondria and steroidogenesis: from individual proteins to functional protein assemblies","volume":"7","author":"Midzak","year":"2016","journal-title":"Front. Endocrinol. (Lausanne)."},{"key":"10.1194\/jlr.R085324_bib42","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1126\/science.2581316","article-title":"A vital stain for the Golgi apparatus","volume":"228","author":"Lipsky","year":"1985","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib43","doi-asserted-by":"crossref","first-page":"2865","DOI":"10.1021\/bi00126a004","article-title":"Determination of the transbilayer distribution of fluorescent lipid analogues by nonradiative fluorescence resonance energy transfer","volume":"31","author":"Wolf","year":"1992","journal-title":"Biochemistry."},{"key":"10.1194\/jlr.R085324_bib44","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1083\/jcb.144.4.673","article-title":"Genetic evidence for ATP-dependent endoplasmic reticulum-to-Golgi apparatus trafficking of ceramide for sphingomyelin synthesis in Chinese hamster ovary cells","volume":"144","author":"Fukasawa","year":"1999","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib45","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1083\/jcb.200704091","article-title":"Pre- and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis","volume":"179","author":"Halter","year":"2007","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib46","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1038\/nature02188","article-title":"Molecular machinery for non-vesicular trafficking of ceramide","volume":"426","author":"Hanada","year":"2003","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib47","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/s11010-005-9044-z","article-title":"Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide","volume":"286","author":"Hanada","year":"2006","journal-title":"Mol. Cell. Biochem."},{"key":"10.1194\/jlr.R085324_bib48","doi-asserted-by":"crossref","first-page":"30279","DOI":"10.1074\/jbc.M605032200","article-title":"Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT","volume":"281","author":"Kawano","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib49","doi-asserted-by":"crossref","first-page":"33787","DOI":"10.1074\/jbc.273.50.33787","article-title":"Mammalian cell mutants resistant to a sphingomyelin-directed cytolysin. Genetic and biochemical evidence for complex formation of the LCB1 protein with the LCB2 protein for serine palmitoyltransferase","volume":"273","author":"Hanada","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib50","doi-asserted-by":"crossref","first-page":"29938","DOI":"10.1074\/jbc.M004470200","article-title":"Reconstitution of ATP- and cytosol-dependent transport of de novo synthesized ceramide to the site of sphingomyelin synthesis in semi-intact cells","volume":"275","author":"Funakoshi","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib51","doi-asserted-by":"crossref","first-page":"12642","DOI":"10.1074\/jbc.274.18.12642","article-title":"Characterization of a novel type of serine\/threonine kinase that specifically phosphorylates the human Goodpasture antigen","volume":"274","author":"Raya","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib52","doi-asserted-by":"crossref","first-page":"40392","DOI":"10.1074\/jbc.M002769200","article-title":"Goodpasture antigen-binding protein, the kinase that phosphorylates the Good\u00adpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis","volume":"275","author":"Raya","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib53","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1034\/j.1600-0854.2004.00071.x","article-title":"Phosphoinositide recognition domains","volume":"4","author":"Lemmon","year":"2003","journal-title":"Traffic."},{"key":"10.1194\/jlr.R085324_bib54","doi-asserted-by":"crossref","first-page":"1519","DOI":"10.1016\/j.celrep.2015.07.054","article-title":"Lipid cooperativity as a general membrane-recruitment principle for PH domains","volume":"12","author":"Vonkova","year":"2015","journal-title":"Cell Reports."},{"key":"10.1194\/jlr.R085324_bib55","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/S0960-9822(02)00779-0","article-title":"Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components","volume":"12","author":"Levine","year":"2002","journal-title":"Curr. Biol."},{"key":"10.1194\/jlr.R085324_bib56","doi-asserted-by":"crossref","first-page":"33706","DOI":"10.1074\/jbc.M112.367730","article-title":"Structural basis for the Golgi association by the pleckstrin homology domain of the ceramide trafficking protein (CERT)","volume":"287","author":"Sugiki","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib57","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1038\/ncb1119","article-title":"FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P","volume":"6","author":"Godi","year":"2004","journal-title":"Nat. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib58","doi-asserted-by":"crossref","first-page":"18650","DOI":"10.1074\/jbc.M111.233015","article-title":"Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain","volume":"286","author":"He","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib59","doi-asserted-by":"crossref","first-page":"e79590","DOI":"10.1371\/journal.pone.0079590","article-title":"Crystal structure of the pleckstrin homology domain from the ceramide transfer protein: implications for conformational change upon ligand binding","volume":"8","author":"Prashek","year":"2013","journal-title":"PLoS One."},{"key":"10.1194\/jlr.R085324_bib60","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1038\/msb.2010.87","article-title":"A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae","volume":"6","author":"Gallego","year":"2010","journal-title":"Mol. Syst. Biol."},{"key":"10.1194\/jlr.R085324_bib61","doi-asserted-by":"crossref","first-page":"16682","DOI":"10.1074\/jbc.M800799200","article-title":"Decreased ceramide transport protein (CERT) function alters sphingomyelin production following UVB irradiation","volume":"283","author":"Charruyer","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib62","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/S0968-0004(99)01362-6","article-title":"START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins","volume":"24","author":"Ponting","year":"1999","journal-title":"Trends Biochem. Sci."},{"key":"10.1194\/jlr.R085324_bib63","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1530\/JOE-11-0313","article-title":"The mammalian START domain protein family in lipid transport in health and disease","volume":"212","author":"Clark","year":"2012","journal-title":"J. Endocrinol."},{"key":"10.1194\/jlr.R085324_bib64","doi-asserted-by":"crossref","first-page":"e19521","DOI":"10.1371\/journal.pone.0019521","article-title":"Comparative structural analysis of lipid binding START domains","volume":"6","author":"Thorsell","year":"2011","journal-title":"PLoS One."},{"key":"10.1194\/jlr.R085324_bib65","doi-asserted-by":"crossref","first-page":"6488","DOI":"10.1074\/jbc.M409290200","article-title":"CERT mediates intermembrane transfer of various molecular species of ceramides","volume":"280","author":"Kumagai","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib66","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1073\/pnas.0709191105","article-title":"Structural basis for specific lipid recognition by CERT responsible for nonvesicular trafficking of ceramide","volume":"105","author":"Kudo","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.R085324_bib67","doi-asserted-by":"crossref","first-page":"6681","DOI":"10.1074\/jbc.R115.685859","article-title":"Dancing protein clouds: the strange biology and chaotic physics of intrinsically disordered proteins","volume":"291","author":"Uversky","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib68","doi-asserted-by":"crossref","first-page":"6696","DOI":"10.1074\/jbc.R115.695056","article-title":"Modulation of intrinsically disordered protein function by post-translational modifications","volume":"291","author":"Bah","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib69","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1093\/emboj\/cdg201","article-title":"A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP","volume":"22","author":"Loewen","year":"2003","journal-title":"EMBO J."},{"key":"10.1194\/jlr.R085324_bib70","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.cell.2015.06.043","article-title":"The BioPlex network: A systematic exploration of the human interactome","volume":"162","author":"Huttlin","year":"2015","journal-title":"Cell."},{"key":"10.1194\/jlr.R085324_bib71","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1016\/j.bbalip.2016.02.009","article-title":"VAP, a versatile access point for the endoplasmic reticulum: review and analysis of FFAT-like motifs in the VAPome","volume":"1861","author":"Murphy","year":"2016","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib72","doi-asserted-by":"crossref","first-page":"10748","DOI":"10.1074\/jbc.M113.528380","article-title":"Pho\u00adsphoregulation of the ceramide transport protein CERT at serine 315 in the interaction with VAMP-associated protein (VAP) for inter-organelle trafficking of ceramide in mammalian cells","volume":"289","author":"Kumagai","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib73","doi-asserted-by":"crossref","first-page":"17758","DOI":"10.1074\/jbc.M702291200","article-title":"Interorganelle trafficking of ceramide is regulated by phosphorylation-dependent cooperativity between the PH and START domains of CERT","volume":"282","author":"Kumagai","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib74","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1083\/jcb.200612017","article-title":"Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein","volume":"178","author":"Fugmann","year":"2007","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib75","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1091\/mbc.e08-07-0669","article-title":"Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin","volume":"20","author":"Tomishige","year":"2009","journal-title":"Mol. Biol. Cell."},{"key":"10.1194\/jlr.R085324_bib76","doi-asserted-by":"crossref","first-page":"14217","DOI":"10.1074\/jbc.M117.780007","article-title":"Interaction between the PH and START domains of ceramide transfer protein competes with phosphatidylinositol 4-phosphate binding by the PH domain","volume":"292","author":"Prashek","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib77","doi-asserted-by":"crossref","first-page":"6584","DOI":"10.1074\/jbc.M707691200","article-title":"Protein phosphatase 2Cepsilon is an endoplasmic reticulum integral membrane protein that dephosphorylates the ceramide transport protein CERT to enhance its association with organelle membranes","volume":"283","author":"Saito","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib78","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1038\/nature14135","article-title":"Deciphering Developmental Disorders Study. Large-scale discovery of novel genetic causes of developmental disorders","volume":"519","year":"2015","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib79","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/j.cell.2006.09.026","article-title":"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks","volume":"127","author":"Olsen","year":"2006","journal-title":"Cell."},{"key":"10.1194\/jlr.R085324_bib80","doi-asserted-by":"crossref","first-page":"36369","DOI":"10.1074\/jbc.M604935200","article-title":"Phosphatidylinositol 4-kinase IIIbeta regulates the transport of ceramide between the endoplasmic reticulum and Golgi","volume":"281","author":"T\u00f3th","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib81","doi-asserted-by":"crossref","first-page":"3871","DOI":"10.1091\/mbc.e08-05-0498","article-title":"Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport","volume":"19","author":"Peretti","year":"2008","journal-title":"Mol. Biol. Cell."},{"key":"10.1194\/jlr.R085324_bib82","doi-asserted-by":"crossref","first-page":"4141","DOI":"10.1091\/mbc.e10-05-0424","article-title":"Oxysterol binding protein-dependent activation of sphingomyelin synthesis in the Golgi apparatus requires phosphatidylinositol 4-kinase IIalpha","volume":"21","author":"Banerji","year":"2010","journal-title":"Mol. Biol. Cell."},{"key":"10.1194\/jlr.R085324_bib83","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1074\/jbc.M115.682997","article-title":"Oxysterol-binding protein activation at endoplasmic reticulum-Golgi contact sites reorganizes phosphatidylinositol 4-phosphate pools","volume":"291","author":"Goto","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib84","doi-asserted-by":"crossref","first-page":"1736","DOI":"10.15252\/embj.201696048","article-title":"Sphingolipid metabolic flow controls phosphoinositide turnover at the trans-Golgi network","volume":"36","author":"Capasso","year":"2017","journal-title":"EMBO J."},{"key":"10.1194\/jlr.R085324_bib85","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.tcb.2013.01.009","article-title":"Inositol lipid regulation of lipid transfer in specialized membrane domains","volume":"23","author":"Kim","year":"2013","journal-title":"Trends Cell Biol."},{"key":"10.1194\/jlr.R085324_bib86","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/0005-2760(91)90002-Y","article-title":"Functional reconstitution of sphingomyelin synthase in Chinese hamster ovary cell membranes","volume":"1086","author":"Hanada","year":"1991","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib87","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/sj.emboj.7600034","article-title":"Identification of a family of animal sphingomyelin synthases","volume":"23","author":"Huitema","year":"2004","journal-title":"EMBO J."},{"key":"10.1194\/jlr.R085324_bib88","doi-asserted-by":"crossref","first-page":"25811","DOI":"10.1074\/jbc.M412052200","article-title":"Rapid transbilayer movement of ceramides in phospholipid vesicles and in human erythrocytes","volume":"280","author":"L\u00f3pez-Montero","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib89","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1194\/jlr.M022491","article-title":"Molecular simulation of rapid translocation of cholesterol, diacylglycerol, and ceramide in model raft and nonraft membranes","volume":"53","author":"Bennett","year":"2012","journal-title":"J. Lipid Res."},{"key":"10.1194\/jlr.R085324_bib90","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.cplett.2011.11.057","article-title":"Rapid flip-flop motions of diacylglycerol and ceramide in phospholipid bilayers","volume":"522","author":"Ogushi","year":"2012","journal-title":"Chem. Phys. Lett."},{"key":"10.1194\/jlr.R085324_bib91","doi-asserted-by":"crossref","first-page":"16798","DOI":"10.1016\/S0021-9258(19)84776-2","article-title":"cDNA cloning and expression of oxysterol-binding protein, an oligomer with a potential leucine zipper","volume":"264","author":"Dawson","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib92","doi-asserted-by":"crossref","first-page":"9046","DOI":"10.1016\/S0021-9258(18)81900-7","article-title":"Purification of oxysterol binding protein from hamster liver cytosol","volume":"264","author":"Dawson","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib93","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1042\/BJ20100263","article-title":"Functional implications of sterol transport by the oxysterol-binding protein gene family","volume":"429","author":"Ngo","year":"2010","journal-title":"Biochem. J."},{"key":"10.1194\/jlr.R085324_bib94","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1093\/genetics\/157.3.1117","article-title":"Overlapping functions of the yeast oxysterol-binding protein homologues","volume":"157","author":"Beh","year":"2001","journal-title":"Genetics."},{"key":"10.1194\/jlr.R085324_bib95","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1038\/nature03923","article-title":"Structural mechanism for sterol sensing and transport by OSBP-related proteins","volume":"437","author":"Im","year":"2005","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib96","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1083\/jcb.200510084","article-title":"Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides","volume":"173","author":"Raychaudhuri","year":"2006","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib97","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1083\/jcb.201104062","article-title":"Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers","volume":"195","author":"de Saint-Jean","year":"2011","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib98","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1016\/j.str.2013.05.007","article-title":"Structure of Osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins","volume":"21","author":"Tong","year":"2013","journal-title":"Structure."},{"key":"10.1194\/jlr.R085324_bib99","doi-asserted-by":"crossref","first-page":"830","DOI":"10.1016\/j.cell.2013.09.056","article-title":"A four-step cycle driven by PI(4)P hydrolysis directs sterol\/PI(4)P exchange by the ER-Golgi tether OSBP","volume":"155","author":"Mesmin","year":"2013","journal-title":"Cell."},{"key":"10.1194\/jlr.R085324_bib100","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1126\/science.aab1346","article-title":"Phosphatidylserine transport by ORP\/Osh proteins is driven by phosphatidylinositol 4-phosphate","volume":"349","author":"Moser von Filseck","year":"2015","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib101","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1126\/science.aab1370","article-title":"PI4P\/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contacts","volume":"349","author":"Chung","year":"2015","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib102","doi-asserted-by":"crossref","first-page":"e35588","DOI":"10.7554\/eLife.35588","article-title":"SAC1 degrades its lipid substrate PtdIns4P in the endoplasmic reticulum to maintain a steep chemical gradient with donor membranes","volume":"7","author":"Zewe","year":"2018","journal-title":"eLife."},{"key":"10.1194\/jlr.R085324_bib103","doi-asserted-by":"crossref","first-page":"5934","DOI":"10.1074\/jbc.M409566200","article-title":"Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction","volume":"280","author":"Amarilio","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib104","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.devcel.2015.04.028","article-title":"Phosphatidylinositol-phosphatidic acid exchange by Nir2 at ER-PM contact sites maintains phosphoinositide signaling competence","volume":"33","author":"Kim","year":"2015","journal-title":"Dev. Cell."},{"key":"10.1194\/jlr.R085324_bib105","doi-asserted-by":"crossref","first-page":"14438","DOI":"10.1074\/jbc.M117.791467","article-title":"Dynamics and energetics of the mammalian phosphatidylinositol transfer protein phospholipid exchange cycle","volume":"292","author":"Grabon","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib106","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1038\/ncb1221","article-title":"Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function","volume":"7","author":"Litvak","year":"2005","journal-title":"Nat. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib107","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1038\/embor.2013.113","article-title":"The phosphatidylinositol-transfer protein Nir2 binds phosphatidic acid and positively regulates phosphoinositide signalling","volume":"14","author":"Kim","year":"2013","journal-title":"EMBO Rep."},{"key":"10.1194\/jlr.R085324_bib108","doi-asserted-by":"crossref","first-page":"14289","DOI":"10.1074\/jbc.M114.621375","article-title":"Phosphatidylinositol 4,5-bisphosphate homeostasis regulated by nir2 and nir3 proteins at endoplasmic reticulum-plasma membrane junctions","volume":"290","author":"Chang","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib109","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1038\/nature12430","article-title":"Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins","volume":"501","author":"Maeda","year":"2013","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib110","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1038\/s41467-017-00861-5","article-title":"ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P 2) and regulate its level at the plasma membrane","volume":"8","author":"Ghai","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1194\/jlr.R085324_bib111","doi-asserted-by":"crossref","first-page":"1797","DOI":"10.1083\/jcb.201710095","article-title":"PI(4,5)P2 controls plasma membrane PI4P and PS levels via ORP5\/8 recruitment to ER-PM contact sites","volume":"217","author":"Sohn","year":"2018","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib112","doi-asserted-by":"crossref","first-page":"800","DOI":"10.15252\/embr.201541108","article-title":"ORP5\/ORP8 localize to endoplasmic reticulum-mitochondria contacts and are involved in mitochondrial function","volume":"17","author":"Galmes","year":"2016","journal-title":"EMBO Rep."},{"key":"10.1194\/jlr.R085324_bib113","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1042\/BJ20070176","article-title":"The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-hydroxycholesterol in an evolutionarily conserved pocket","volume":"405","author":"Suchanek","year":"2007","journal-title":"Biochem. J."},{"key":"10.1194\/jlr.R085324_bib114","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1091\/mbc.e08-09-0905","article-title":"Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function","volume":"20","author":"Ngo","year":"2009","journal-title":"Mol. Biol. Cell."},{"key":"10.1194\/jlr.R085324_bib115","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1083\/jcb.200905007","article-title":"Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues","volume":"187","author":"Schulz","year":"2009","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib116","doi-asserted-by":"crossref","first-page":"5636","DOI":"10.1074\/jbc.RA117.000596","article-title":"Oxysterol-binding protein homologs mediate sterol transport from the endoplasmic reticulum to mitochondria in yeast","volume":"293","author":"Tian","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib117","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/0005-2760(81)90025-4","article-title":"Intermembrane phospholipid fluxes catalyzed by bovine brain phospholipid exchange protein","volume":"664","author":"Kasper","year":"1981","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib118","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1186\/1471-2105-15-222","article-title":"Identification and phylogenetic analyses of VASt, an uncharacterized protein domain associated with lipid-binding domains in Eukaryotes","volume":"15","author":"Khafif","year":"2014","journal-title":"BMC Bioinformatics."},{"key":"10.1194\/jlr.R085324_bib119","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1042\/BST20150275","article-title":"Lipid transfer proteins do their thing anchored at membrane contact sites... but what is their thing?","volume":"44","author":"Wong","year":"2016","journal-title":"Biochem. Soc. Trans."},{"key":"10.1194\/jlr.R085324_bib120","doi-asserted-by":"crossref","first-page":"824","DOI":"10.15252\/embr.201540229","article-title":"Structural insight into the TRIAP1\/PRELI-like domain family of mitochondrial phospholipid transfer complexes","volume":"16","author":"Miliara","year":"2015","journal-title":"EMBO Rep."},{"key":"10.1194\/jlr.R085324_bib121","doi-asserted-by":"crossref","first-page":"813","DOI":"10.15252\/embr.201540137","article-title":"Structural basis of intramitochondrial phosphatidic acid transport mediated by Ups1-Mdm35 complex","volume":"16","author":"Yu","year":"2015","journal-title":"EMBO Rep."},{"key":"10.1194\/jlr.R085324_bib122","doi-asserted-by":"crossref","first-page":"7922","DOI":"10.1038\/ncomms8922","article-title":"Structural and mechanistic insights into phospholipid transfer by Ups1-Mdm35 in mitochondria","volume":"6","author":"Watanabe","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1194\/jlr.R085324_bib123","doi-asserted-by":"crossref","first-page":"8793","DOI":"10.1038\/s41598-017-09205-1","article-title":"Identification of the N-terminal transmembrane domain of StarD7 and its importance for mitochondrial outer membrane localization and phosphatidylcholine transfer","volume":"7","author":"Horibata","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1194\/jlr.R085324_bib124","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1126\/science.1225625","article-title":"Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein","volume":"338","author":"Connerth","year":"2012","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib125","doi-asserted-by":"crossref","first-page":"15205","DOI":"10.1074\/jbc.M111.338665","article-title":"Role for two conserved intermembrane space proteins, Ups1p and Ups2p, [corrected] in intra-mitochondrial phospholipid trafficking","volume":"287","author":"Tamura","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib126","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.cmet.2013.07.008","article-title":"TRIAP1\/PRELI complexes prevent apoptosis by mediating intramitochondrial transport of phosphatidic acid","volume":"18","author":"Potting","year":"2013","journal-title":"Cell Metab."},{"key":"10.1194\/jlr.R085324_bib127","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1083\/jcb.201602007","article-title":"MICOS and phospholipid transfer by Ups2-Mdm35 organize membrane lipid synthesis in mitochondria","volume":"213","author":"Aaltonen","year":"2016","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib128","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1083\/jcb.201601082","article-title":"Phosphatidylserine transport by Ups2-Mdm35 in respiration-active mitochondria","volume":"214","author":"Miyata","year":"2016","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib129","doi-asserted-by":"crossref","first-page":"2111","DOI":"10.1194\/jlr.R016675","article-title":"Early steps in steroidogenesis: intracellular cholesterol trafficking","volume":"52","author":"Miller","year":"2011","journal-title":"J. Lipid Res."},{"key":"10.1194\/jlr.R085324_bib130","doi-asserted-by":"crossref","first-page":"4615","DOI":"10.1016\/S0021-9258(18)89115-3","article-title":"Specificity of the glycolipid transfer protein from pig brain","volume":"260","author":"Yamada","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib131","doi-asserted-by":"crossref","first-page":"9634","DOI":"10.1016\/S0021-9258(19)38716-2","article-title":"Primary structure of glycolipid transfer protein from pig brain","volume":"265","author":"Abe","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib132","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1038\/nature02856","article-title":"Structural basis for glycosphingolipid transfer specificity","volume":"430","author":"Malinina","year":"2004","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib133","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1038\/nature06097","article-title":"Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide","volume":"449","author":"D'Angelo","year":"2007","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib134","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1038\/nature12423","article-title":"Vesicular and non-vesicular transport feed distinct glycosylation pathways in the Golgi","volume":"501","author":"D'Angelo","year":"2013","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib135","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1038\/nature12332","article-title":"Non-vesicular trafficking by a ceramide-1-phosphate transfer protein regulates eicosanoids","volume":"500","author":"Simanshu","year":"2013","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib136","doi-asserted-by":"crossref","first-page":"E856","DOI":"10.1073\/pnas.1719709115","article-title":"Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites","volume":"115","author":"Tong","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.R085324_bib137","doi-asserted-by":"crossref","first-page":"5522","DOI":"10.1074\/jbc.RA118.001881","article-title":"Structural basis of sterol binding and transport by a yeast StARkin domain","volume":"293","author":"Jentsch","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib138","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/S0968-0004(00)01664-9","article-title":"GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins","volume":"25","author":"Doerks","year":"2000","journal-title":"Trends Biochem. Sci."},{"key":"10.1194\/jlr.R085324_bib139","doi-asserted-by":"crossref","first-page":"1391","DOI":"10.1016\/S1097-2765(03)00486-6","article-title":"Crystal structure of a phosphoinositide phosphatase, MTMR2: insights into myotubular myopathy and Charcot-Marie-Tooth syndrome","volume":"12","author":"Begley","year":"2003","journal-title":"Mol. Cell."},{"key":"10.1194\/jlr.R085324_bib140","doi-asserted-by":"crossref","first-page":"e31019","DOI":"10.7554\/eLife.31019","article-title":"GRAM domain proteins specialize functionally distinct ER-PM contact sites in human cells","volume":"7","author":"Besprozvannaya","year":"2018","journal-title":"eLife."},{"key":"10.1194\/jlr.R085324_bib141","doi-asserted-by":"crossref","first-page":"e07253","DOI":"10.7554\/eLife.07253","article-title":"A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport","volume":"4","author":"Gatta","year":"2015","journal-title":"eLife."},{"key":"10.1194\/jlr.R085324_bib142","doi-asserted-by":"crossref","first-page":"2679","DOI":"10.1083\/jcb.201610032","article-title":"Sterol transporters at membrane contact sites regulate TORC1 and TORC2 signaling","volume":"216","author":"Murley","year":"2017","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib143","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1083\/jcb.201502033","article-title":"Ltc1 is an ER-localized sterol transporter and a component of ER-mitochondria and ER-vacuole contacts","volume":"209","author":"Murley","year":"2015","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib144","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.celrep.2015.06.022","article-title":"Lam6 regulates the extent of contacts between organelles","volume":"12","author":"Elbaz-Alon","year":"2015","journal-title":"Cell Reports."},{"key":"10.1194\/jlr.R085324_bib145","doi-asserted-by":"crossref","first-page":"e98002","DOI":"10.15252\/embj.201798002","article-title":"Molecular basis for sterol transport by StART-like lipid transfer domains","volume":"37","author":"Horenkamp","year":"2018","journal-title":"EMBO J."},{"key":"10.1194\/jlr.R085324_bib146","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1096\/fj.05-4581hyp","article-title":"Diverse membrane-associated proteins contain a novel SMP domain","volume":"20","author":"Lee","year":"2006","journal-title":"FASEB J."},{"key":"10.1194\/jlr.R085324_bib147","doi-asserted-by":"crossref","first-page":"1927","DOI":"10.1093\/bioinformatics\/btq326","article-title":"Homology of SMP domains to the TULIP superfamily of lipid-binding proteins provides a structural basis for lipid exchange between ER and mitochondria","volume":"26","author":"Kopec","year":"2010","journal-title":"Bioinformatics."},{"key":"10.1194\/jlr.R085324_bib148","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/j.devcel.2012.11.004","article-title":"ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology","volume":"23","author":"Manford","year":"2012","journal-title":"Dev. Cell."},{"key":"10.1194\/jlr.R085324_bib149","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1016\/j.cell.2013.05.026","article-title":"PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins","volume":"153","author":"Giordano","year":"2013","journal-title":"Cell."},{"key":"10.1194\/jlr.R085324_bib150","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1016\/j.bbalip.2015.12.003","article-title":"SMP-domain proteins at membrane contact sites: Structure and function","volume":"1861","author":"Reinisch","year":"2016","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib151","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1038\/nature13269","article-title":"Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer","volume":"510","author":"Schauder","year":"2014","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib152","doi-asserted-by":"crossref","first-page":"eaah6171","DOI":"10.1126\/science.aah6171","article-title":"Lipid transport by TMEM24 at ER-plasma membrane contacts regulates pulsatile insulin secretion","volume":"355","author":"Lees","year":"2017","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib153","doi-asserted-by":"crossref","first-page":"E3179","DOI":"10.1073\/pnas.1422363112","article-title":"Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly","volume":"112","author":"AhYoung","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.R085324_bib154","doi-asserted-by":"crossref","first-page":"1857","DOI":"10.15252\/embr.201642706","article-title":"Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex","volume":"17","author":"Jeong","year":"2016","journal-title":"EMBO Rep."},{"key":"10.1194\/jlr.R085324_bib155","doi-asserted-by":"crossref","first-page":"E9502","DOI":"10.1073\/pnas.1715592114","article-title":"Crystal structures of Mmm1 and Mdm12-Mmm1 reveal mechanistic insight into phospholipid trafficking at ER-mitochondria contact sites","volume":"114","author":"Jeong","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.R085324_bib156","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1083\/jcb.201704119","article-title":"Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES","volume":"217","author":"Kawano","year":"2018","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib157","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/s13062-017-0174-5","article-title":"Of yeast, mice and men: MAMs come in two flavors","volume":"12","author":"Herrera-Cruz","year":"2017","journal-title":"Biol. Direct."},{"key":"10.1194\/jlr.R085324_bib158","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1038\/nrm3440","article-title":"Endoplasmic reticulum-mitochondria contacts: function of the junction","volume":"13","author":"Rowland","year":"2012","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib159","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1126\/science.aan6009","article-title":"ER-mitochondria tethering by PDZD8 regulates Ca(2+) dynamics in mammalian neurons","volume":"358","author":"Hirabayashi","year":"2017","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib160","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1242\/jcs.085118","article-title":"A conserved membrane-binding domain targets proteins to organelle contact sites","volume":"125","author":"Toulmay","year":"2012","journal-title":"J. Cell Sci."},{"key":"10.1194\/jlr.R085324_bib161","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1083\/jcb.201606059","article-title":"An inducible ER-Golgi tether facilitates ceramide transport to alleviate lipotoxicity","volume":"216","author":"Liu","year":"2017","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib162","first-page":"376","article-title":"Osh proteins regulate COPII-mediated vesicular transport of ceramide from the endoplasmic reticulum in budding yeast","volume":"127","author":"Kajiwara","year":"2014","journal-title":"J. Cell Sci."},{"key":"10.1194\/jlr.R085324_bib163","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1038\/nsmb1197","article-title":"Crystal structure of cholesteryl ester transfer protein reveals a long tunnel and four bound lipid molecules","volume":"14","author":"Qiu","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1194\/jlr.R085324_bib164","first-page":"507","article-title":"Structure of human phosphatidylcholine transfer protein in complex with its ligand","volume":"9","author":"Roderick","year":"2002","journal-title":"Nat. Struct. Biol."},{"key":"10.1194\/jlr.R085324_bib165","doi-asserted-by":"crossref","first-page":"798","DOI":"10.1126\/science.aar1886","article-title":"Lipopolysaccharide is transported to the cell surface by a membrane-to-membrane protein bridge","volume":"359","author":"Sherman","year":"2018","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib166","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1038\/cdd.2015.160","article-title":"NDPK-D (NM23\u2013H4)-mediated externalization of cardiolipin enables elimination of depolarized mitochondria by mitophagy","volume":"23","author":"Kagan","year":"2016","journal-title":"Cell Death Differ."},{"key":"10.1194\/jlr.R085324_bib167","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1038\/ncb2837","article-title":"Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells","volume":"15","author":"Chu","year":"2013","journal-title":"Nat. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib168","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1016\/j.jmb.2006.10.028","article-title":"Cardiolipin clusters and membrane domain formation induced by mitochondrial proteins","volume":"365","author":"Epand","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1194\/jlr.R085324_bib169","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1074\/jbc.M112.408633","article-title":"Dual function of mitochondrial Nm23-H4 protein in phosphotransfer and intermembrane lipid transfer: a cardiolipin-dependent switch","volume":"288","author":"Schlattner","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib170","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.bbalip.2004.08.007","article-title":"Structure and function of the NPC2 protein","volume":"1685","author":"Vanier","year":"2004","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib171","doi-asserted-by":"crossref","first-page":"2298","DOI":"10.1126\/science.290.5500.2298","article-title":"Identification of HE1 as the second gene of Niemann-Pick C disease","volume":"290","author":"Naureckiene","year":"2000","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib172","doi-asserted-by":"crossref","first-page":"2512","DOI":"10.1073\/pnas.0437840100","article-title":"Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease","volume":"100","author":"Friedland","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.R085324_bib173","doi-asserted-by":"crossref","first-page":"31594","DOI":"10.1074\/jbc.M602765200","article-title":"Mechanism of cholesterol transfer from the Niemann-Pick type C2 protein to model membranes supports a role in lysosomal cholesterol transport","volume":"281","author":"Cheruku","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib174","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1016\/j.cell.2016.05.022","article-title":"Structural insights into the Niemann-Pick C1 (NPC1)-mediated cholesterol transfer and Ebola infection","volume":"165","author":"Gong","year":"2016","journal-title":"Cell."},{"key":"10.1194\/jlr.R085324_bib175","doi-asserted-by":"crossref","first-page":"24367","DOI":"10.1074\/jbc.M002184200","volume":"275","author":"Davies","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib176","doi-asserted-by":"crossref","first-page":"2295","DOI":"10.1126\/science.290.5500.2295","article-title":"Transmembrane molecular pump activity of Niemann-Pick C1 protein","volume":"290","author":"Davies","year":"2000","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib177","doi-asserted-by":"crossref","first-page":"21604","DOI":"10.1074\/jbc.271.35.21604","article-title":"Intracellular trafficking of cholesterol monitored with a cyclodextrin","volume":"271","author":"Neufeld","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib178","doi-asserted-by":"crossref","first-page":"4266","DOI":"10.1074\/jbc.273.7.4266","article-title":"Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane","volume":"273","author":"Underwood","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib179","first-page":"5500","article-title":"STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER","volume":"126","author":"Alpy","year":"2013","journal-title":"J. Cell Sci."},{"key":"10.1194\/jlr.R085324_bib180","doi-asserted-by":"crossref","first-page":"1412","DOI":"10.15252\/embj.201695917","article-title":"STARD3 mediates endoplasmic reticulum-to-endosome cholesterol transport at membrane contact sites","volume":"36","author":"Wilhelm","year":"2017","journal-title":"EMBO J."},{"key":"10.1194\/jlr.R085324_bib181","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1091\/mbc.e02-08-0459","article-title":"The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct","volume":"14","author":"Johansson","year":"2003","journal-title":"Mol. Biol. Cell."},{"key":"10.1194\/jlr.R085324_bib182","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1083\/jcb.200811005","article-title":"Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning","volume":"185","author":"Rocha","year":"2009","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib183","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/j.devcel.2016.05.005","article-title":"Annexin A1 tethers membrane contact sites that mediate ER to endosome cholesterol transport","volume":"37","author":"Eden","year":"2016","journal-title":"Dev. Cell."},{"key":"10.1194\/jlr.R085324_bib184","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1016\/j.celrep.2017.05.028","article-title":"Oxysterol-binding protein-related protein 1L regulates cholesterol egress from the endo-lysosomal system","volume":"19","author":"Zhao","year":"2017","journal-title":"Cell Reports."},{"key":"10.1194\/jlr.R085324_bib185","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1126\/science.1233508","article-title":"Impaired alpha-TTP-PIPs interaction underlies familial vitamin E deficiency","volume":"340","author":"Kono","year":"2013","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib186","doi-asserted-by":"crossref","first-page":"2776","DOI":"10.1021\/ja01131a021","article-title":"The diffusion coefficient of calcium chloride in aqueous solution at 25\u00b0","volume":"74","author":"Robinson","year":"1952","journal-title":"J. Am. Chem. Soc."},{"key":"10.1194\/jlr.R085324_bib187","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/0304-4157(92)90007-W","article-title":"Spontaneous lipid transfer between organized lipid assemblies","volume":"1113","author":"Brown","year":"1992","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib188","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1038\/nature04162","article-title":"Interfaces and the driving force of hydrophobic assembly","volume":"437","author":"Chandler","year":"2005","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib189","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.tibs.2016.11.004","article-title":"Speed limits for nonvesicular intracellular sterol transport","volume":"42","author":"Dittman","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"10.1194\/jlr.R085324_bib190","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1242\/jcs.194191","article-title":"Diverting CERT-mediated ceramide transport to mitochondria triggers Bax-dependent apoptosis","volume":"130","author":"Jain","year":"2017","journal-title":"J. Cell Sci."},{"key":"10.1194\/jlr.R085324_bib191","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1088\/0143-0807\/27\/2\/018","article-title":"Chemical potential\u2013a quantity in search of recognition","volume":"27","author":"Job","year":"2006","journal-title":"Eur. J. Phys."},{"key":"10.1194\/jlr.R085324_bib192","doi-asserted-by":"crossref","first-page":"12422","DOI":"10.1073\/pnas.220418097","article-title":"Condensed complexes, rafts, and the chemical activity of cholesterol in membranes","volume":"97","author":"Radhakrishnan","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.R085324_bib193","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.ceb.2006.06.012","article-title":"Intracellular sterol transport and distribution","volume":"18","author":"Maxfield","year":"2006","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib194","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/j.plipres.2008.03.001","article-title":"Cholesterol homeostasis and the escape tendency (activity) of plasma membrane cholesterol","volume":"47","author":"Lange","year":"2008","journal-title":"Prog. Lipid Res."},{"key":"10.1194\/jlr.R085324_bib195","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1083\/jcb.100.1.27","article-title":"Intracellular translocation of fluorescent sphingolipids in cultured fibroblasts: endogenously synthesized sphingomyelin and glucocerebroside analogues pass through the Golgi apparatus en route to the plasma membrane","volume":"100","author":"Lipsky","year":"1985","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib196","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1083\/jcb.151.3.507","article-title":"Evidence for segregation of sphingomyelin and cholesterol during formation of COPI-coated vesicles","volume":"151","author":"Br\u00fcgger","year":"2000","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib197","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1016\/j.bpj.2015.12.043","article-title":"Lipid interactions and organization in complex bilayer membranes","volume":"110","author":"Engberg","year":"2016","journal-title":"Biophys. J."},{"key":"10.1194\/jlr.R085324_bib198","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1083\/jcb.201607086","article-title":"Raft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogs","volume":"216","author":"Kinoshita","year":"2017","journal-title":"J. Cell Biol."},{"key":"10.1194\/jlr.R085324_bib199","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.bbamem.2015.12.008","article-title":"The importance of hydrogen bonding in sphingomyelin's membrane interactions with co-lipids","volume":"1858","author":"Slotte","year":"2016","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib200","doi-asserted-by":"crossref","first-page":"11179","DOI":"10.1073\/pnas.94.21.11179","article-title":"Sphingomyelin depletion in cultured cells blocks proteolysis of sterol regulatory element binding proteins at site 1","volume":"94","author":"Scheek","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.R085324_bib201","doi-asserted-by":"crossref","first-page":"34028","DOI":"10.1074\/jbc.M005151200","article-title":"Reduction of sphingomyelin level without accumulation of ceramide in Chinese hamster ovary cells affects detergent-resistant membrane domains and enhances cellular cholesterol efflux to methyl-beta -cyclodextrin","volume":"275","author":"Fukasawa","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib202","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.02882","article-title":"Three pools of plasma membrane cholesterol and their relation to cholesterol homeostasis","volume":"3","author":"Das","year":"2014","journal-title":"eLife."},{"key":"10.1194\/jlr.R085324_bib203","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.bbamem.2008.08.016","article-title":"Lipid lateral diffusion and membrane heterogeneity","volume":"1788","author":"Lindblom","year":"2009","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib204","doi-asserted-by":"crossref","first-page":"8840","DOI":"10.1021\/bi970145r","article-title":"Measurement of spontaneous transfer and transbilayer movement of BODIPY-labeled lipids in lipid vesicles","volume":"36","author":"Bai","year":"1997","journal-title":"Biochemistry."},{"key":"10.1194\/jlr.R085324_bib205","doi-asserted-by":"crossref","first-page":"65","DOI":"10.3389\/fphys.2014.00065","article-title":"Cholesterol binding to ion channels","volume":"5","author":"Levitan","year":"2014","journal-title":"Front. Physiol."},{"key":"10.1194\/jlr.R085324_bib206","article-title":"Cambridge University Press","author":"Schr\u00f6dinger","year":"1944","journal-title":"Cambridge, UK."},{"key":"10.1194\/jlr.R085324_bib207","doi-asserted-by":"crossref","first-page":"e88124","DOI":"10.1371\/journal.pone.0088124","article-title":"Establishment of HeLa cell mutants deficient in sphingolipid-related genes using TALENs","volume":"9","author":"Yamaji","year":"2014","journal-title":"PLoS One."},{"key":"10.1194\/jlr.R085324_bib208","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.3390\/ijms17101761","article-title":"Role of intracellular lipid logistics in the preferential usage of very long chain-ceramides in glucosylceramide","volume":"17","author":"Yamaji","year":"2016","journal-title":"Int. J. Mol. Sci."},{"key":"10.1194\/jlr.R085324_bib209","doi-asserted-by":"crossref","first-page":"3234","DOI":"10.1091\/mbc.e14-03-0851","article-title":"Systematic lipidomic analysis of yeast protein kinase and phosphatase mutants reveals novel insights into regulation of lipid homeostasis","volume":"25","author":"da Silveira Dos Santos","year":"2014","journal-title":"Mol. Biol. Cell."},{"key":"10.1194\/jlr.R085324_bib210","doi-asserted-by":"crossref","first-page":"eaan4368","DOI":"10.1126\/science.aan4368","article-title":"The target landscape of clinical kinase drugs","volume":"358","author":"Klaeger","year":"2017","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib211","doi-asserted-by":"crossref","first-page":"R41","DOI":"10.1186\/gb-2004-5-6-r41","article-title":"START lipid\/sterol-binding domains are amplified in plants and are predominantly associated with homeodomain transcription factors","volume":"5","author":"Schrick","year":"2004","journal-title":"Genome Biol."},{"key":"10.1194\/jlr.R085324_bib212","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.bcp.2013.02.016","article-title":"Oxysterol-binding proteins: functions in cell regulation beyond lipid metabolism","volume":"86","author":"Weber-Boyvat","year":"2013","journal-title":"Biochem. Pharmacol."},{"key":"10.1194\/jlr.R085324_bib213","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.1111\/j.1471-4159.2010.06673.x","article-title":"The ceramide transporter and the Goodpasture antigen binding protein: one protein\u2013one function?","volume":"113","author":"Mencarelli","year":"2010","journal-title":"J. Neurochem."},{"key":"10.1194\/jlr.R085324_bib214","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1016\/j.bbalip.2014.12.011","article-title":"Phosphatidylinositol transfer proteins and instructive regulation of lipid kinase biology","volume":"1851","author":"Grabon","year":"2015","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.R085324_bib215","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.plipres.2015.10.004","article-title":"The orchestra of lipid-transfer proteins at the crossroads between metabolism and signaling","volume":"61","author":"Chiapparino","year":"2016","journal-title":"Prog. Lipid Res."},{"key":"10.1194\/jlr.R085324_bib216","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/347561a0","article-title":"An essential role for a phospholipid transfer protein in yeast Golgi function","volume":"347","author":"Bankaitis","year":"1990","journal-title":"Nature."},{"key":"10.1194\/jlr.R085324_bib217","doi-asserted-by":"crossref","first-page":"1472","DOI":"10.1126\/science.1107710","article-title":"OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1\/2 activation","volume":"307","author":"Wang","year":"2005","journal-title":"Science."},{"key":"10.1194\/jlr.R085324_bib218","doi-asserted-by":"crossref","first-page":"3806","DOI":"10.1074\/jbc.RA117.001558","article-title":"Oxysterol-binding protein-related protein 5 (ORP5) promotes cell proliferation by activation of mTORC1 signaling","volume":"293","author":"Du","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib219","doi-asserted-by":"crossref","first-page":"43994","DOI":"10.1074\/jbc.M104884200","article-title":"A novel inhibitor of ceramide trafficking from the endoplasmic reticulum to the site of sphingomyelin synthesis","volume":"276","author":"Yasuda","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib220","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1016\/j.bmc.2017.02.026","article-title":"Iminosugar-based ceramide mimicry for the design of new CERT START domain ligands","volume":"25","author":"Santos","year":"2017","journal-title":"Bioorg. Med. Chem."},{"key":"10.1194\/jlr.R085324_bib221","doi-asserted-by":"crossref","first-page":"4139","DOI":"10.1016\/j.bmcl.2012.04.058","article-title":"Identification of small-molecule inhibitors of the steroidogenic acute regulatory protein (STARD1) by structure-based design","volume":"22","author":"Akula","year":"2012","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1194\/jlr.R085324_bib222","doi-asserted-by":"crossref","first-page":"4252","DOI":"10.1128\/JVI.03546-12","article-title":"Oxysterol-binding protein family I is the target of minor enviroxime-like compounds","volume":"87","author":"Arita","year":"2013","journal-title":"J. Virol."},{"key":"10.1194\/jlr.R085324_bib223","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1038\/nchembio.625","article-title":"Natural products reveal cancer cell dependence on oxysterol-binding proteins","volume":"7","author":"Burgett","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"10.1194\/jlr.R085324_bib224","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1016\/j.celrep.2014.12.054","article-title":"Itraconazole inhibits enterovirus replication by targeting the oxysterol-binding protein","volume":"10","author":"Strating","year":"2015","journal-title":"Cell Reports."},{"key":"10.1194\/jlr.R085324_bib225","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2013a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"10.1194\/jlr.R085324_bib226","doi-asserted-by":"crossref","first-page":"14713","DOI":"10.1073\/pnas.2136684100","article-title":"Crystal structure of human alpha-tocopherol transfer protein bound to its ligand: implications for ataxia with vitamin E deficiency","volume":"100","author":"Min","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.R085324_bib227","doi-asserted-by":"crossref","first-page":"32656","DOI":"10.1074\/jbc.272.51.32656","article-title":"Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity","volume":"272","author":"Arakane","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib228","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1210\/me.2014-1028","article-title":"The contribution of serine 194 phosphorylation to steroidogenic acute regulatory protein function","volume":"28","author":"Sasaki","year":"2014","journal-title":"Mol. Endocrinol."},{"key":"10.1194\/jlr.R085324_bib229","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.mce.2008.10.009","article-title":"Hormonal activation of a kinase cascade localized at the mitochondria is required for StAR protein activity","volume":"300","author":"Poderoso","year":"2009","journal-title":"Mol. Cell. Endocrinol."},{"key":"10.1194\/jlr.R085324_bib230","doi-asserted-by":"crossref","first-page":"3624","DOI":"10.1091\/mbc.e12-04-0283","article-title":"Multisite phosphorylation of oxysterol-binding protein regulates sterol binding and activation of sphingomyelin synthesis","volume":"23","author":"Goto","year":"2012","journal-title":"Mol. Biol. Cell."},{"key":"10.1194\/jlr.R085324_bib231","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1006\/excr.2001.5460","article-title":"Clofibrate-induced relocation of phosphatidylcholine transfer protein to mitochondria in endothelial cells","volume":"274","author":"de Brouwer","year":"2002","journal-title":"Exp. Cell Res."},{"key":"10.1194\/jlr.R085324_bib232","doi-asserted-by":"crossref","first-page":"22447","DOI":"10.1074\/jbc.M201532200","article-title":"The Golgi localization of phosphatidylinositol transfer protein beta requires the protein kinase C-dependent phosphorylation of serine 262 and is essential for maintaining plasma membrane sphingomyelin levels","volume":"277","author":"van Tiel","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib233","doi-asserted-by":"crossref","first-page":"27436","DOI":"10.1074\/jbc.M413330200","article-title":"StarD10, a START domain protein overexpressed in breast cancer, functions as a phospholipid transfer protein","volume":"280","author":"Olayioye","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.R085324_bib234","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/j.yexcr.2014.10.019","article-title":"OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity","volume":"331","author":"Weber-Boyvat","year":"2015","journal-title":"Exp. Cell Res."}],"updated-by":[{"DOI":"10.1194\/jlr.r085324err","type":"erratum","label":"Erratum","source":"publisher","updated":{"date-parts":[[2018,10,1]],"date-time":"2018-10-01T00:00:00Z","timestamp":1538352000000}}],"container-title":["Journal of Lipid Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022227520330479?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022227520330479?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1194\/jlr.R085324","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,7,7]],"date-time":"2024-07-07T10:46:07Z","timestamp":1720349167000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022227520330479"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,8]]},"references-count":234,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2018,8]]}},"alternative-id":["S0022227520330479"],"URL":"https:\/\/doi.org\/10.1194\/jlr.r085324","relation":{},"ISSN":["0022-2275"],"issn-type":[{"value":"0022-2275","type":"print"}],"subject":[],"published":{"date-parts":[[2018,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Lipid transfer proteins rectify inter-organelle flux and accurately deliver lipids at membrane contact sites","name":"articletitle","label":"Article Title"},{"value":"Journal of Lipid Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1194\/jlr.R085324","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2018 Hanada","name":"copyright","label":"Copyright"}]}}