{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["285(18)"],"submitter":["Kim S"],"pubmed_abstract":["The integral endoplasmic reticulum (ER)-membrane protein VAP-B interacts with various lipid-transfer/binding proteins containing an FFAT motif through its N-terminal MSP domain. A genetic mutation within its MSP domain, P56S, was identified in familial forms of motor neuron diseases. This mutation induces the formation of insoluble VAP-B(P56S) protein aggregates by an unknown mechanism. In this study, we defined the structural requirements for VAP-B oligomerization and demonstrated their contribution for VAP-B(P56S) aggregation and neurotoxicity. We show that the oligomerization of VAP-B is mainly mediated by its coiled-coil domain and that the GXXXG dimerization motif within the transmembrane domain mediates transmembrane domains self-association but is insufficient to drive VAP-B oligome"],"journal":["The Journal of biological chemistry"],"pagination":["13839-49"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2859547"],"repository":["biostudies-literature"],"pubmed_title":["Structural requirements for VAP-B oligomerization and their implication in amyotrophic lateral sclerosis-associated VAP-B(P56S) neurotoxicity."],"pmcid":["PMC2859547"],"pubmed_authors":["Kim S","Leal SS","Ben Halevy D","Gomes CM","Lev S"],"additional_accession":[]},"is_claimable":false,"name":"Structural requirements for VAP-B oligomerization and their implication in amyotrophic lateral sclerosis-associated VAP-B(P56S) neurotoxicity.","description":"The integral endoplasmic reticulum (ER)-membrane protein VAP-B interacts with various lipid-transfer/binding proteins containing an FFAT motif through its N-terminal MSP domain. A genetic mutation within its MSP domain, P56S, was identified in familial forms of motor neuron diseases. This mutation induces the formation of insoluble VAP-B(P56S) protein aggregates by an unknown mechanism. In this study, we defined the structural requirements for VAP-B oligomerization and demonstrated their contribution for VAP-B(P56S) aggregation and neurotoxicity. We show that the oligomerization of VAP-B is mainly mediated by its coiled-coil domain and that the GXXXG dimerization motif within the transmembrane domain mediates transmembrane domains self-association but is insufficient to drive VAP-B oligome","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Apr","modification":"2025-04-19T06:32:53.91Z","creation":"2019-03-27T00:30:21Z"},"accession":"S-EPMC2859547","cross_references":{"pubmed":["20207736"],"doi":["10.1074/jbc.M109.097345","10.1074/jbc.m109.097345"]}}