{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T18:07:49Z","timestamp":1791223669432,"version":"4.1.0"},"reference-count":38,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2016,2,1]],"date-time":"2016-02-01T00:00:00Z","timestamp":1454284800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,12]],"date-time":"2020-09-12T00:00:00Z","timestamp":1599868800000},"content-version":"vor","delay-in-days":1685,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2016,2]]},"DOI":"10.1074\/jbc.m115.703710","type":"journal-article","created":{"date-parts":[[2015,12,4]],"date-time":"2015-12-04T02:49:46Z","timestamp":1449197386000},"page":"3124-3134","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":60,"title":["Interaction between a Domain of the Negative Regulator of the Ras-ERK Pathway, SPRED1 Protein, and the GTPase-activating Protein-related Domain of Neurofibromin Is Implicated in Legius Syndrome and Neurofibromatosis Type 1"],"prefix":"10.1016","volume":"291","author":[{"given":"Yasuko","family":"Hirata","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hilde","family":"Brems","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mayu","family":"Suzuki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mitsuhiro","family":"Kanamori","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masahiro","family":"Okada","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rimpei","family":"Morita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabel","family":"Llano-Rivas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toyoyuki","family":"Ose","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ludwine","family":"Messiaen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric","family":"Legius","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akihiko","family":"Yoshimura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M115.703710_bib1","doi-asserted-by":"crossref","first-page":"73","DOI":"10.2302\/kjm.58.73","article-title":"Regulation of cytokine signaling by the SOCS and Spred family proteins","volume":"58","author":"Yoshimura","year":"2009","journal-title":"Keio J. Med"},{"key":"10.1074\/jbc.M115.703710_bib2","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1002\/bies.20632","article-title":"Getting a first clue about SPRED functions","volume":"29","author":"Bundschu","year":"2007","journal-title":"BioEssays"},{"key":"10.1074\/jbc.M115.703710_bib3","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/S0006-291X(03)00259-6","article-title":"Molecular cloning of mammalian Spred-3 which suppresses tyrosine kinase-mediated Erk activation","volume":"302","author":"Kato","year":"2003","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M115.703710_bib4","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1111\/j.1365-2443.2005.00886.x","article-title":"The Sprouty-related protein, Spred-1, localizes in a lipid raft\/caveola and inhibits ERK activation in collaboration with caveolin-1","volume":"10","author":"Nonami","year":"2005","journal-title":"Genes Cells"},{"key":"10.1074\/jbc.M115.703710_bib5","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1083\/jcb.152.5.1087","article-title":"Mammalian sprouty-1 and -2 are membrane-anchored phosphoprotein inhibitors of growth factor signaling in endothelial cells","volume":"152","author":"Impagnatiello","year":"2001","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M115.703710_bib6","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1038\/ng2113","article-title":"Germline loss-of-function mutations in SPRED1 cause a neurofibromatosis 1-like phenotype","volume":"39","author":"Brems","year":"2007","journal-title":"Nat. Genet"},{"key":"10.1074\/jbc.M115.703710_bib7","doi-asserted-by":"crossref","first-page":"2111","DOI":"10.1001\/jama.2009.1663","article-title":"Clinical and mutational spectrum of neurofibromatosis type 1-like syndrome","volume":"302","author":"Messiaen","year":"2009","journal-title":"JAMA"},{"key":"10.1074\/jbc.M115.703710_bib8","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1136\/jmg.2008.065243","article-title":"SPRED1 germline mutations caused a neurofibromatosis type 1 overlapping phenotype","volume":"46","author":"Pasmant","year":"2009","journal-title":"J. Med. Genet"},{"key":"10.1074\/jbc.M115.703710_bib9","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1136\/jmg.2008.065474","article-title":"SPRED1 mutations (Legius syndrome): another clinically useful genotype for dissecting the neurofibromatosis type 1 phenotype","volume":"46","author":"Spurlock","year":"2009","journal-title":"J. Med. Genet"},{"key":"10.1074\/jbc.M115.703710_bib10","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1177\/0883073809359540","article-title":"SPRED 1 mutations in a neurofibromatosis clinic","volume":"25","author":"Muram-Zborovski","year":"2010","journal-title":"J. Child Neurol"},{"key":"10.1074\/jbc.M115.703710_bib11","doi-asserted-by":"crossref","first-page":"107","DOI":"10.2302\/kjm.2013-0002-RE","article-title":"Legius syndrome, an update. Molecular pathology of mutations in SPRED1","volume":"62","author":"Brems","year":"2013","journal-title":"Keio J. Med"},{"key":"10.1074\/jbc.M115.703710_bib12","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1038\/onc.2013.587","article-title":"SPRED1, a RAS MAPK pathway inhibitor that causes Legius syndrome, is a tumour suppressor downregulated in paediatric acute myeloblastic leukaemia","volume":"34","author":"Pasmant","year":"2015","journal-title":"Oncogene"},{"key":"10.1074\/jbc.M115.703710_bib13","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1146\/annurev-genom-091212-153523","article-title":"The RASopathies","volume":"14","author":"Rauen","year":"2013","journal-title":"Annu. Rev. Genomics Hum. Genet"},{"key":"10.1074\/jbc.M115.703710_bib14","doi-asserted-by":"crossref","first-page":"6056","DOI":"10.1038\/sj.onc.1209635","article-title":"Spreds, inhibitors of the Ras\/ERK signal transduction, are dysregulated in human hepatocellular carcinoma and linked to the malignant phenotype of tumors","volume":"25","author":"Yoshida","year":"2006","journal-title":"Oncogene"},{"key":"10.1074\/jbc.M115.703710_bib15","doi-asserted-by":"crossref","first-page":"5567","DOI":"10.1038\/sj.onc.1207759","article-title":"The Sprouty-related protein, Spred, inhibits cell motility, metastasis, and Rho-mediated actin reorganization","volume":"23","author":"Miyoshi","year":"2004","journal-title":"Oncogene"},{"key":"10.1074\/jbc.M115.703710_bib16","doi-asserted-by":"crossref","first-page":"4541","DOI":"10.1128\/MCB.01600-06","article-title":"Spreds are essential for embryonic lymphangiogenesis by regulating vascular endothelial growth factor receptor 3 signaling","volume":"27","author":"Taniguchi","year":"2007","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.M115.703710_bib17","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1038\/35088082","article-title":"Spred is a Sprouty-related suppressor of Ras signalling","volume":"412","author":"Wakioka","year":"2001","journal-title":"Nature"},{"key":"10.1074\/jbc.M115.703710_bib18","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1101\/gad.190876.112","article-title":"A shared molecular mechanism underlies the human rasopathies Legius syndrome and neurofibromatosis-1","volume":"26","author":"Stowe","year":"2012","journal-title":"Genes Dev"},{"key":"10.1074\/jbc.M115.703710_bib19","doi-asserted-by":"crossref","first-page":"E1985","DOI":"10.1002\/humu.21404","article-title":"Legius syndrome in fourteen families","volume":"32","author":"Denayer","year":"2011","journal-title":"Hum. Mutat"},{"key":"10.1074\/jbc.M115.703710_bib20","doi-asserted-by":"crossref","first-page":"1538","DOI":"10.1002\/humu.22152","article-title":"Review and update of SPRED1 mutations causing Legius syndrome","volume":"33","author":"Brems","year":"2012","journal-title":"Hum. Mutat"},{"key":"10.1074\/jbc.M115.703710_bib21","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1002\/1098-1004(200006)15:6<541::AID-HUMU6>3.0.CO;2-N","article-title":"Exhaustive mutation analysis of the NF1 gene allows identification of 95% of mutations and reveals a high frequency of unusual splicing defects","volume":"15","author":"Messiaen","year":"2000","journal-title":"Hum. Mutat"},{"key":"10.1074\/jbc.M115.703710_bib22","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1159\/000126545","article-title":"NF1 Mutational Spectrum","volume":"16","author":"Messiaen","year":"2008","journal-title":"Monogr. Hum. Genet"},{"key":"10.1074\/jbc.M115.703710_bib23","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1046\/j.1365-2443.1999.00263.x","article-title":"Cytokine-inducible SH2 protein-3 (CIS3\/SOCS3) inhibits Janus tyrosine kinase by binding through the N-terminal kinase inhibitory region as well as SH2 domain","volume":"4","author":"Sasaki","year":"1999","journal-title":"Genes Cells"},{"key":"10.1074\/jbc.M115.703710_bib24","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1093\/jb\/mvg004","article-title":"CIS1 interacts with the Y532 of the prolactin receptor and suppresses prolactin-dependent STAT5 activation","volume":"133","author":"Endo","year":"2003","journal-title":"J. Biochem"},{"key":"10.1074\/jbc.M115.703710_bib25","doi-asserted-by":"crossref","first-page":"960","DOI":"10.2144\/96206bm03","article-title":"An in vitro assay of \u03b2-galactosidase from yeast","volume":"20","author":"Schneider","year":"1996","journal-title":"BioTechniques"},{"key":"10.1074\/jbc.M115.703710_bib26","doi-asserted-by":"crossref","first-page":"36804","DOI":"10.1074\/jbc.C100386200","article-title":"Identification of a dominant negative mutant of Sprouty that potentiates fibroblast growth factor\u2013but not epidermal growth factor-induced ERK activation","volume":"276","author":"Sasaki","year":"2001","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.703710_bib27","doi-asserted-by":"crossref","first-page":"1648","DOI":"10.1111\/j.1349-7006.2009.01214.x","article-title":"Sprouty4 deficiency potentiates Ras-independent angiogenic signals and tumor growth","volume":"100","author":"Taniguchi","year":"2009","journal-title":"Cancer Sci"},{"key":"10.1074\/jbc.M115.703710_bib28","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1093\/hmg\/ddt014","article-title":"Functional analysis of a duplication (p.E63_D69dup) in the switch II region of HRAS: new aspects of the molecular pathogenesis underlying Costello syndrome","volume":"22","author":"Lorenz","year":"2013","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M115.703710_bib29","doi-asserted-by":"crossref","first-page":"2159","DOI":"10.1002\/prot.24403","article-title":"How good is automated protein docking?","volume":"81","author":"Kozakov","year":"2013","journal-title":"Proteins"},{"key":"10.1074\/jbc.M115.703710_bib30","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/0092-8674(90)90150-D","article-title":"The GAP-related domain of the neurofibromatosis type 1 gene product interacts with ras p21","volume":"63","author":"Martin","year":"1990","journal-title":"Cell"},{"key":"10.1074\/jbc.M115.703710_bib31","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1016\/0092-8674(90)90149-9","article-title":"The catalytic domain of the neurofibromatosis type 1 gene product stimulates ras GTPase and complements ira mutants of S. cerevisiae","volume":"63","author":"Xu","year":"1990","journal-title":"Cell"},{"key":"10.1074\/jbc.M115.703710_bib32","doi-asserted-by":"crossref","first-page":"16409","DOI":"10.1074\/jbc.271.27.16409","article-title":"Structural differences in the minimal catalytic domains of the GTPase-activating proteins p120GAP and neurofibromin","volume":"271","author":"Ahmadian","year":"1996","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.703710_bib33","first-page":"487","article-title":"A conserved alternative splice in the von Recklinghausen neurofibromatosis (NF1) gene produces two neurofibromin isoforms, both of which have GTPase-activating protein activity","volume":"13","author":"Andersen","year":"1993","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.M115.703710_bib34","doi-asserted-by":"crossref","first-page":"1687","DOI":"10.1002\/humu.22162","article-title":"Assessment of the potential pathogenicity of missense mutations identified in the GTPase-activating protein (GAP)-related domain of the neurofibromatosis type-1 (NF1) gene","volume":"33","author":"Thomas","year":"2012","journal-title":"Hum. Mutat"},{"key":"10.1074\/jbc.M115.703710_bib35","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1038\/gim.2015.30","article-title":"Standards and guidelines for the interpretation of sequence variants: a joint consensus recommendation of the American College of Medical Genetics and Genomics and the Association for Molecular Pathology","volume":"17","author":"Richards","year":"2015","journal-title":"Genet. Med"},{"key":"10.1074\/jbc.M115.703710_bib36","doi-asserted-by":"crossref","first-page":"4313","DOI":"10.1093\/emboj\/17.15.4313","article-title":"Structural analysis of the GAP-related domain from neurofibromin and its implications","volume":"17","author":"Scheffzek","year":"1998","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M115.703710_bib37","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1093\/hmg\/7.8.1261","article-title":"Selective disactivation of neurofibromin GAP activity in neurofibromatosis type 1","volume":"7","author":"Klose","year":"1998","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M115.703710_bib38","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1016\/j.febslet.2004.11.114","article-title":"1.15 A crystal structure of the X. tropicalis Spred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family","volume":"579","author":"Harmer","year":"2005","journal-title":"FEBS Lett"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820451397?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820451397?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M115.703710","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T14:14:24Z","timestamp":1641305664000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820451397"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,2]]},"references-count":38,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2016,2]]}},"alternative-id":["S0021925820451397"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m115.703710","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2016,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Interaction between a Domain of the Negative Regulator of the Ras-ERK Pathway, SPRED1 Protein, and the GTPase-activating Protein-related Domain of Neurofibromin Is Implicated in Legius Syndrome and Neurofibromatosis Type 1","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M115.703710","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}