The Atlastin C-terminal Tail is an Amphipathic Helix that Perturbs Bilayer Structure during Endoplasmic Reticulum Homotypic Fusion
dc.citation.journalTitle | The Journal of Biological Chemistry | |
dc.contributor.author | Faust, Joseph E. | |
dc.contributor.author | Desai, Tanvi | |
dc.contributor.author | Verma, Avani | |
dc.contributor.author | Ulengin, Idil | |
dc.contributor.author | Sun, Tzu-Lin | |
dc.contributor.author | Moss, Tyler J. | |
dc.contributor.author | Betancourt, Miguel A. | |
dc.contributor.author | Huang, Huey W. | |
dc.contributor.author | Lee, Tina | |
dc.contributor.author | McNew, James A. | |
dc.date.accessioned | 2015-01-16T16:13:07Z | |
dc.date.available | 2015-01-16T16:13:07Z | |
dc.date.issued | 2015 | |
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.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." <i>The Journal of Biological Chemistry,</i> (2015) American Society for Biochemistry and Molecular Biology: http://dx.doi.org/10.1074/jbc.M114.601823. | |
dc.identifier.doi | http://dx.doi.org/10.1074/jbc.M114.601823 | |
dc.identifier.uri | https://hdl.handle.net/1911/78925 | |
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.subject.keyword | cell compartmentalization | |
dc.subject.keyword | endoplasmic reticulum (ER) | |
dc.subject.keyword | membrane fusion | |
dc.subject.keyword | fluorescence resonance energy transfer (FRET) | |
dc.subject.keyword | phospholipid vesicle | |
dc.subject.keyword | neurodegeneration | |
dc.subject.keyword | membrane structure | |
dc.subject.keyword | GTPase | |
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.type.dcmi | Text | en_US |
dc.type.publication | post-print |
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