{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T06:08:24Z","timestamp":1789020504373,"version":"build-2803163510"},"reference-count":80,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T00:00:00Z","timestamp":1779321600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB1348"],"award-info":[{"award-number":["SFB1348"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["467522186"],"award-info":[{"award-number":["467522186"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB1557"],"award-info":[{"award-number":["SFB1557"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["538651361"],"award-info":[{"award-number":["538651361"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["FOR5815"],"award-info":[{"award-number":["FOR5815"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["386797833"],"award-info":[{"award-number":["386797833"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Cell Biology"],"published-print":{"date-parts":[[2026,8]]},"DOI":"10.1016\/j.ceb.2026.102665","type":"journal-article","created":{"date-parts":[[2026,6,12]],"date-time":"2026-06-12T09:38:32Z","timestamp":1781257112000},"page":"102665","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"special_numbering":"C","title":["I did it my way: the origins of lipid droplet heterogeneity"],"prefix":"10.1016","volume":"101","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8154-555X","authenticated-orcid":false,"given":"Maria","family":"Bohnert","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ceb.2026.102665_bib1","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1146\/annurev-cellbio-012624-031419","article-title":"Lipid droplets big and small: basic mechanisms that make them all","volume":"40","author":"Klemm","year":"2024","journal-title":"Annu Rev Cell Dev Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib2","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202406019","article-title":"Lipid droplets: open questions and conceptual advances around a unique organelle","volume":"224","author":"Henne","year":"2025","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib3","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1146\/annurev-biochem-091724-013733","article-title":"Essential biology of lipid droplets","volume":"94","author":"Farese","year":"2025","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.ceb.2026.102665_bib4","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.tibs.2021.08.007","article-title":"The CYTOLD and ERTOLD pathways for lipid droplet-protein targeting","volume":"47","author":"Olarte","year":"2022","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.ceb.2026.102665_bib5","doi-asserted-by":"crossref","DOI":"10.1016\/j.sbi.2023.102606","article-title":"Structure and function of lipid droplet assembly complexes","volume":"80","author":"Walther","year":"2023","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib6","doi-asserted-by":"crossref","first-page":"1364","DOI":"10.1038\/s41556-022-00974-0","article-title":"Identification of two pathways mediating protein targeting from ER to lipid droplets","volume":"24","author":"Song","year":"2022","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib7","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1083\/jcb.201704122","article-title":"Identification of seipin-linked factors that act as determinants of a lipid droplet subpopulation","volume":"217","author":"Eisenberg-Bord","year":"2018","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib8","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1083\/jcb.201704115","article-title":"Regulation of lipid droplets by metabolically controlled Ldo isoforms","volume":"217","author":"Teixeira","year":"2018","journal-title":"JCB (J Cell Biol)"},{"key":"10.1016\/j.ceb.2026.102665_bib9","doi-asserted-by":"crossref","first-page":"ar3","DOI":"10.1091\/mbc.E25-10-0480","article-title":"Organization of the yeast Seipin complex reveals differential recruitment of regulatory proteins","volume":"37","author":"Klug","year":"2026","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.ceb.2026.102665_sref10","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1016\/j.devcel.2024.01.016","article-title":"A metabolically controlled contact site between vacuoles and lipid droplets in yeast","volume":"59","author":"Diep","year":"2024","journal-title":"Dev Cell"},{"key":"10.1016\/j.ceb.2026.102665_sref11","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1016\/j.devcel.2024.01.014","article-title":"LDO proteins and Vac8 form a vacuole-lipid droplet contact site to enable starvation-induced lipophagy in yeast","volume":"59","author":"\u00c1lvarez-Guerra","year":"2024","journal-title":"Dev Cell"},{"key":"10.1016\/j.ceb.2026.102665_sref12","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2025.116475","article-title":"The Myo2 adaptor Ldm1 and its receptor Ldo16 mediate actin-dependent lipid droplet motility","volume":"44","author":"Zhao","year":"2025","journal-title":"Cell Rep"},{"key":"10.1016\/j.ceb.2026.102665_bib13","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.devcel.2019.10.006","article-title":"LDAF1 and seipin form a lipid droplet assembly complex","volume":"51","author":"Chung","year":"2019","journal-title":"Dev Cell"},{"key":"10.1016\/j.ceb.2026.102665_bib14","doi-asserted-by":"crossref","DOI":"10.3390\/cells8030268","article-title":"Promethin is a conserved seipin partner protein","volume":"8","author":"Castro","year":"2019","journal-title":"Cells"},{"key":"10.1016\/j.ceb.2026.102665_bib15","doi-asserted-by":"crossref","DOI":"10.1016\/j.ibmb.2020.103512","article-title":"CG32803 is the fly homolog of LDAF1 and influences lipid storage in vivo","volume":"133","author":"Chartschenko","year":"2021","journal-title":"Insect Biochem Mol Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib16","series-title":"Mechanism for oil-phase separation by the lipid droplet assembly complex","author":"Malia","year":"2025"},{"key":"10.1016\/j.ceb.2026.102665_sref17","doi-asserted-by":"crossref","first-page":"eadr9755","DOI":"10.1126\/science.adr9755","article-title":"Adipogenin promotes the development of lipid droplets by binding a dodecameric seipin complex","volume":"390","author":"Li","year":"2025","journal-title":"Science"},{"key":"10.1016\/j.ceb.2026.102665_bib18","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.semcdb.2020.04.012","article-title":"New friends for seipin - implications of seipin partner proteins in the life cycle of lipid droplets","volume":"108","author":"Bohnert","year":"2020","journal-title":"Semin Cell Dev Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib19","doi-asserted-by":"crossref","first-page":"37713","DOI":"10.1074\/jbc.M304025200","article-title":"Adipocyte protein S3-12 coats nascent lipid droplets","volume":"278","author":"Wolins","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ceb.2026.102665_bib20","doi-asserted-by":"crossref","first-page":"19146","DOI":"10.1074\/jbc.M500978200","article-title":"S3- 12, Adipophilin, and TIP47 package lipid in adipocytes","volume":"280","author":"Wolins","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ceb.2026.102665_bib21","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0090386","article-title":"On the formation of lipid droplets in human adipocytes: the organization of the perilipin-vimentin cortex","volume":"9","author":"Heid","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.ceb.2026.102665_bib22","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1091\/mbc.E18-08-0534","article-title":"Dual binding motifs underpin the hierarchical association of perilipins1-3 with lipid droplets","volume":"30","author":"Ajjaji","year":"2019","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.ceb.2026.102665_bib23","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1016\/j.molcel.2019.09.011","article-title":"MIGA2 Links Mitochondria, the ER, and Lipid Droplets and Promotes De Novo Lipogenesis in Adipocytes","volume":"76","author":"Freyre","year":"2019","journal-title":"Mol Cell"},{"key":"10.1016\/j.ceb.2026.102665_sref24","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2024.114093","article-title":"Perilipin membrane integration determines lipid droplet heterogeneity in differentiating adipocytes","volume":"43","author":"Majchrzak","year":"2024","journal-title":"Cell Rep"},{"key":"10.1016\/j.ceb.2026.102665_sref25","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202403064","article-title":"Surface tension-driven sorting of human perilipins on lipid droplets","volume":"223","author":"Dias Ara\u00fajo","year":"2024","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib26","doi-asserted-by":"crossref","first-page":"1594","DOI":"10.1038\/ncomms2581","article-title":"Perilipin1 promotes unilocular lipid droplet formation through the activation of Fsp27 in adipocytes","volume":"4","author":"Sun","year":"2013","journal-title":"Nat Commun"},{"key":"10.1016\/j.ceb.2026.102665_bib27","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/j.cub.2018.02.020","article-title":"Architecture of lipid droplets in endoplasmic reticulum is determined by phospholipid intrinsic curvature","volume":"28","author":"Choudhary","year":"2018","journal-title":"Curr Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib28","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.devcel.2019.05.003","article-title":"Membrane asymmetry imposes directionality on lipid droplet emergence from the ER","volume":"50","author":"Chorlay","year":"2019","journal-title":"Dev Cell"},{"key":"10.1016\/j.ceb.2026.102665_bib29","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1016\/j.cmet.2011.07.013","article-title":"Phosphatidylcholine synthesis for lipid droplet expansion is mediated by localized activation of CTP:phosphocholine cytidylyltransferase","volume":"14","author":"Krahmer","year":"2011","journal-title":"Cell Metab"},{"key":"10.1016\/j.ceb.2026.102665_bib30","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.devcel.2013.01.013","article-title":"Triacylglycerol synthesis enzymes mediate lipid droplet growth by relocalizing from the ER to lipid droplets","volume":"24","author":"Wilfling","year":"2013","journal-title":"Dev Cell"},{"key":"10.1016\/j.ceb.2026.102665_bib31","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.devcel.2018.04.012","article-title":"PCYT1A regulates phosphatidylcholine homeostasis from the inner nuclear membrane in response to membrane stored curvature elastic stress","volume":"45","author":"Haider","year":"2018","journal-title":"Dev Cell"},{"key":"10.1016\/j.ceb.2026.102665_sref32","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1038\/s41467-023-36375-6","article-title":"Cholesterol esters form supercooled lipid droplets whose nucleation is facilitated by triacylglycerols","volume":"14","author":"Dumesnil","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.ceb.2026.102665_bib33","doi-asserted-by":"crossref","first-page":"5332","DOI":"10.1016\/S0021-9258(19)69203-3","article-title":"The order-disorder transition of the core cholesteryl esters of human plasma low density lipoprotein. A proton nuclear magnetic resonance study","volume":"256","author":"Kroon","year":"1981","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ceb.2026.102665_bib34","doi-asserted-by":"crossref","first-page":"16866","DOI":"10.1073\/pnas.1903642116","article-title":"Liquid-crystalline phase transitions in lipid droplets are related to cellular states and specific organelle association","volume":"116","author":"Mahamid","year":"2019","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.ceb.2026.102665_bib35","doi-asserted-by":"crossref","first-page":"25440","DOI":"10.1073\/pnas.1916248116","article-title":"Universal phase behaviors of intracellular lipid droplets","volume":"116","author":"Shimobayashi","year":"2019","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.ceb.2026.102665_bib36","doi-asserted-by":"crossref","first-page":"2774","DOI":"10.1038\/s44318-025-00423-2","article-title":"Nuclear envelope-associated lipid droplets are enriched in cholesteryl esters and increase during inflammatory signaling","volume":"44","author":"Szkalisity","year":"2025","journal-title":"EMBO J"},{"key":"10.1016\/j.ceb.2026.102665_bib37","doi-asserted-by":"crossref","first-page":"17065","DOI":"10.1074\/jbc.M800401200","article-title":"Structural and biochemical properties of lipid particles from the yeast Saccharomyces cerevisiae","volume":"283","author":"Czabany","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ceb.2026.102665_bib38","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202205053","article-title":"Triglyceride lipolysis triggers liquid crystalline phases in lipid droplets and alters the LD proteome","volume":"221","author":"Rogers","year":"2022","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib39","first-page":"4067","article-title":"Perilipin family members preferentially sequester to either triacylglycerol-specific or cholesteryl-esterspecific intracellular lipid storage droplets","volume":"125","author":"Hsieh","year":"2012","journal-title":"J Cell Sci"},{"key":"10.1016\/j.ceb.2026.102665_bib40","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0105047","article-title":"The proteome of cholesteryl-ester-enriched versus triacylglycerol-enriched lipid droplets","volume":"9","author":"Khor","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.ceb.2026.102665_bib41","doi-asserted-by":"crossref","first-page":"3199","DOI":"10.1083\/jcb.201610013","article-title":"Pet10p is a yeast perilipin that stabilizes lipid droplets and promotes their assembly","volume":"216","author":"Gao","year":"2017","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_sref42","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202303026","article-title":"Tld1 is a regulator of triglyceride lipolysis that demarcates a lipid droplet subpopulation","volume":"223","author":"Speer","year":"2024","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_sref43","doi-asserted-by":"crossref","first-page":"1902","DOI":"10.1038\/s41556-025-01790-y","article-title":"FSP1-mediated lipid droplet quality control prevents neutral lipid peroxidation and ferroptosis","volume":"27","author":"Lange","year":"2025","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib44","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/j.devcel.2019.07.021","article-title":"Drosophila snazarus regulates a lipid droplet population at plasma membrane-droplet contacts in adipocytes","volume":"50","author":"Ugrankar","year":"2019","journal-title":"Dev Cell"},{"key":"10.1016\/j.ceb.2026.102665_sref45","doi-asserted-by":"crossref","DOI":"10.1038\/s41586-025-10064-4","article-title":"CLCC1 promotes hepatic neutral lipid flux and nuclear pore complex assembly","author":"Mathiowetz","year":"2026","journal-title":"Nature"},{"key":"10.1016\/j.ceb.2026.102665_sref46","doi-asserted-by":"crossref","DOI":"10.1038\/s41586-026-10161-y","article-title":"CLCC1 governs ER bilayer equilibration to maintain lipid homeostasis","author":"Wu","year":"2026","journal-title":"Nature"},{"key":"10.1016\/j.ceb.2026.102665_bib47","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1016\/j.cmet.2021.05.006","article-title":"TMEM41B acts as an ER scramblase required for lipoprotein biogenesis and lipid homeostasis","volume":"33","author":"Huang","year":"2021","journal-title":"Cell Metab"},{"key":"10.1016\/j.ceb.2026.102665_bib48","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202011071","article-title":"Retinyl esters form lipid droplets independently of triacylglycerol and seipin","volume":"220","author":"Molenaar","year":"2021","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib49","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1038\/nature22369","article-title":"Applying systems-level spectral imaging and analysis to reveal the organelle interactome","volume":"546","author":"Valm","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.ceb.2026.102665_bib50","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.1038\/s41467-018-03957-8","article-title":"Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact","volume":"9","author":"Shai","year":"2018","journal-title":"Nat Commun"},{"key":"10.1016\/j.ceb.2026.102665_bib51","doi-asserted-by":"crossref","DOI":"10.1038\/s41580-025-00945-x","article-title":"Heterogeneity, dynamics and organelle interactions of lipid droplets","author":"Henne","year":"2026","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib52","article-title":"ORP5 localizes to ER\u2013lipid droplet contacts and regulates the level of PI(4)P on lipid droplets","volume":"219","author":"Du","year":"2020","journal-title":"JCB (J Cell Biol)"},{"key":"10.1016\/j.ceb.2026.102665_bib53","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202112107","article-title":"ORP5 and ORP8 orchestrate lipid droplet biogenesis and maintenance at ER\u2013mitochondria contact sites","volume":"221","author":"Guyard","year":"2022","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib54","doi-asserted-by":"crossref","first-page":"1967","DOI":"10.1007\/s00018-014-1786-x","article-title":"Ligand-dependent localization and function of ORP\u2013VAP complexes at membrane contact sites","volume":"72","author":"Weber-Boyvat","year":"2015","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.ceb.2026.102665_bib55","doi-asserted-by":"crossref","first-page":"3625","DOI":"10.1083\/jcb.201807019","article-title":"VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites","volume":"217","author":"Kumar","year":"2018","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib56","article-title":"A possible role of VPS13B in the formation of golgi-lipid droplet contacts associating with the ER","volume":"6","author":"Du","year":"2023","journal-title":"Contact"},{"key":"10.1016\/j.ceb.2026.102665_bib57","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1038\/s41467-021-21525-5","article-title":"An ESCRT-dependent step in fatty acid transfer from lipid droplets to mitochondria through VPS13D\u2212TSG101 interactions","volume":"12","author":"Wang","year":"2021","journal-title":"Nat Commun"},{"key":"10.1016\/j.ceb.2026.102665_bib58","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202207022","article-title":"Mitoguardin-2\u2013mediated lipid transfer preserves mitochondrial morphology and lipid droplet formation","volume":"221","author":"Hong","year":"2022","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib59","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1074\/jbc.M114.604744","article-title":"The interplay of protein kinase A and perilipin 5 regulates cardiac lipolysis","volume":"290","author":"Pollak","year":"2015","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ceb.2026.102665_bib60","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-025-07934-2","article-title":"Pex3 promotes formation of peroxisome-peroxisome and peroxisome-lipid droplet contact sites","volume":"15","author":"Amado","year":"2025","journal-title":"Sci Rep"},{"key":"10.1016\/j.ceb.2026.102665_bib61","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1083\/jcb.201201139","article-title":"The FATP1-DGAT2 complex facilitates lipid droplet expansion at the ERlipid droplet interface","volume":"198","author":"Xu","year":"2012","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_sref62","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1016\/j.devcel.2023.05.006","article-title":"PLIN5 interacts with FATP4 at membrane contact sites to promote lipid droplet-to-mitochondria fatty acid transport","volume":"58","author":"Miner","year":"2023","journal-title":"Dev Cell"},{"key":"10.1016\/j.ceb.2026.102665_sref63","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1038\/s41556-024-01457-0","article-title":"Functional multi-organelle units control inflammatory lipid metabolism of macrophages","volume":"26","author":"Zimmermann","year":"2024","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib64","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.15252\/embj.201694914","article-title":"Mfn2 is critical for brown adipose tissue thermogenic function","volume":"36","author":"Boutant","year":"2017","journal-title":"EMBO J"},{"key":"10.1016\/j.ceb.2026.102665_bib65","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1016\/j.cellbi.2009.06.011","article-title":"Lipid droplets interact with mitochondria using SNAP23","volume":"33","author":"J\u00e4gerstr\u00f6m","year":"2009","journal-title":"Cell Biol Int"},{"key":"10.1016\/j.ceb.2026.102665_bib66","doi-asserted-by":"crossref","first-page":"16724","DOI":"10.1074\/jbc.RA118.004049","article-title":"Long-chain acyl-CoA synthetase 1 interacts with key proteins that activate and direct fatty acids into niche hepatic pathways","volume":"293","author":"Young","year":"2018","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ceb.2026.102665_bib67","doi-asserted-by":"crossref","first-page":"2159","DOI":"10.1194\/jlr.M017939","article-title":"Perilipin 5, a lipid droplet-associated protein, provides physical and metabolic linkage to mitochondria","volume":"52","author":"Wang","year":"2011","journal-title":"J Lipid Res"},{"key":"10.1016\/j.ceb.2026.102665_sref68","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.devcel.2023.01.007","article-title":"Rab8a as a mitochondrial receptor for lipid droplets in skeletal muscle","volume":"58","author":"Ouyang","year":"2023","journal-title":"Dev Cell"},{"key":"10.1016\/j.ceb.2026.102665_sref69","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1038\/s42255-024-01025-8","article-title":"A spatiotemporal proteomic map of human adipogenesis","volume":"6","author":"Klingelhuber","year":"2024","journal-title":"Nat Metab"},{"key":"10.1016\/j.ceb.2026.102665_sref70","doi-asserted-by":"crossref","DOI":"10.1038\/s41556-026-01890-3","article-title":"Mitochondria contact lipid droplets through the mitochondrial import complex binding to lipid metabolism enzyme Ayr1","author":"Heinen","year":"2026","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib71","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1083\/jcb.201507122","article-title":"PML isoform II plays a critical role in nuclear lipid droplet formation","volume":"212","author":"Ohsaki","year":"2016","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib72","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1038\/s41467-019-08411-x","article-title":"Nuclear lipid droplets derive from a lipoprotein precursor and regulate phosphatidylcholine synthesis","volume":"10","author":"So\u0142tysik","year":"2019","journal-title":"Nat Commun"},{"key":"10.1016\/j.ceb.2026.102665_bib73","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202005026","article-title":"Nuclear lipid droplets form in the inner nuclear membrane in a seipin-independent manner","volume":"220","author":"So\u0142tysik","year":"2021","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib74","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1016\/j.cell.2018.05.047","article-title":"The inner nuclear membrane is a metabolically active territory that generates nuclear lipid droplets","volume":"174","author":"Romanauska","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.ceb.2026.102665_bib75","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1038\/nature07976","article-title":"Autophagy regulates lipid metabolism","volume":"458","author":"Singh","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.ceb.2026.102665_bib76","first-page":"32443","volume":"117","author":"Schulze","year":"2020"},{"key":"10.1016\/j.ceb.2026.102665_sref77","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1038\/s41556-023-01178-w","article-title":"The Troyer syndrome protein spartin mediates selective autophagy of lipid droplets","volume":"25","author":"Chung","year":"2023","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.ceb.2026.102665_bib78","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1091\/mbc.e13-08-0448","article-title":"Lipid droplet autophagy in the yeast Saccharomyces cerevisiae","volume":"25","author":"van Zutphen","year":"2014","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.ceb.2026.102665_bib79","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1016\/j.bbalip.2017.07.009","article-title":"The perilipin family of lipid droplet proteins: gatekeepers of intracellular lipolysis","volume":"1862","author":"Sztalryd","year":"2017","journal-title":"Biochim Biophys Acta Mol Cell Biol Lipids"},{"key":"10.1016\/j.ceb.2026.102665_bib80","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.devcel.2015.06.007","article-title":"Protein crowding is a determinant of lipid droplet protein composition","volume":"34","author":"Kory","year":"2015","journal-title":"Dev Cell"}],"container-title":["Current Opinion in Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067426000530?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067426000530?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,7,24]],"date-time":"2026-07-24T12:06:30Z","timestamp":1784894790000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0955067426000530"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8]]},"references-count":80,"alternative-id":["S0955067426000530"],"URL":"https:\/\/doi.org\/10.1016\/j.ceb.2026.102665","relation":{},"ISSN":["0955-0674"],"issn-type":[{"value":"0955-0674","type":"print"}],"subject":[],"published":{"date-parts":[[2026,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"I did it my way: the origins of lipid droplet heterogeneity","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Cell Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ceb.2026.102665","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Author(s). Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"102665"}}