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dc.contributor.authorFaust, Joseph E.
Desai, Tanvi
Verma, Avani
Ulengin, Idil
Sun, Tzu-Lin
Moss, Tyler J.
Betancourt, Miguel A.
Huang, Huey W.
Lee, Tina
McNew, James A.
dc.date.accessioned 2015-01-16T16:13:07Z
dc.date.available 2015-01-16T16:13:07Z
dc.date.issued 2015
dc.identifier.citation Faust, Joseph E., Desai, Tanvi, Verma, Avani, et al.. "The Atlastin C-terminal Tail is an Amphipathic Helix that Perturbs Bilayer Structure during Endoplasmic Reticulum Homotypic Fusion." The Journal of Biological Chemistry, (2015) American Society for Biochemistry and Molecular Biology: http://dx.doi.org/10.1074/jbc.M114.601823.
dc.identifier.urihttps://hdl.handle.net/1911/78925
dc.description.abstract Fusion of tubular membranes is required to form three-way junctions found in reticular subdomains of the endoplasmic reticulum (ER). The large GTPase Atlastin has recently been shown to drive ER membrane fusion and three-way junction formation. The mechanism of Atlastin-mediated membrane fusion is distinct from SNARE-mediated and many details remain unclear. In particular, the role of the amphipathic C-terminal tail of Atlastin is still unknown. We have found that a peptide corresponding to the Atlastin C-terminal tail binds to membranes as a parallel alpha helix, induces bilayer thinning, and increases acyl chain disorder. The function of the C-terminal tail is conserved in human Atlastin. Mutations in the C-terminal tail decrease fusion activity in vitro, but not GTPase activity, and impair Atlastin function in vivo. In the context of unstable lipid bilayers, the requirement for the C-terminal tail is abrogated. These data suggest that the C-terminal tail of Atlastin locally destabilizes bilayers to facilitate membrane fusion.
dc.language.iso eng
dc.publisher American Society for Biochemistry and Molecular Biology
dc.rights This is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by the American Society for Biochemistry and Molecular Biology.
dc.title The Atlastin C-terminal Tail is an Amphipathic Helix that Perturbs Bilayer Structure during Endoplasmic Reticulum Homotypic Fusion
dc.type Journal article
dc.contributor.funder National Institutes of Health
dc.contributor.funder Virginia and L.E. Simmons Family Foundation
dc.contributor.funder Hamill Foundation
dc.contributor.funder Welch Foundation
dc.citation.journalTitle The Journal of Biological Chemistry
dc.subject.keywordcell compartmentalization
endoplasmic reticulum (ER)
membrane fusion
fluorescence resonance energy transfer (FRET)
phospholipid vesicle
neurodegeneration
membrane structure
GTPase
dc.type.dcmi Text
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M114.601823
dc.identifier.pmcid PMC4335215
dc.identifier.pmid 25555915
dc.identifier.grantID GM101377 (National Institutes of Health)
dc.identifier.grantID GM55203 (National Institutes of Health)
dc.identifier.grantID C-0991 (Welch Foundation)
dc.identifier.grantID GM107285 (National Institutes of Health)
dc.type.publication post-print


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