The complexin C-terminal amphipathic helix stabilizes the fusion pore open state by sculpting membranes-Reference-Cited by-同舟云学术

The complexin C-terminal amphipathic helix stabilizes the fusion pore open state by sculpting membranes

Published:2022-02 Issue:2 Volume:29 Page:97-107
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Courtney Kevin C.^ORCID,Wu Lanxi,Mandal Taraknath,Swift Mark^ORCID,Zhang Zhao,Alaghemandi Mohammad,Wu Zhenyong,Bradberry Mazdak M.^ORCID,Deo Claire^ORCID,Lavis Luke D.^ORCID,Volkmann Niels,Hanein Dorit^ORCID,Cui Qiang,Bao Huan,Chapman Edwin R.^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

https://www.nature.com/articles/s41594-021-00716-0.pdf

Reference91 articles.

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2. Mcmahon, H. T., Missler, M., Li, C. & Sudhof, T. C. Complexins—cytosolic proteins that regulate snap receptor function. Cell 83, 111–119 (1995).

3. Reim, K. et al. Complexins regulate a late step in Ca2+-dependent neurotransmitter release. Cell 104, 71–81 (2001).

4. Ishizuka, T., Saisu, H., Odani, S. & Abe, T. Synaphin—a protein associated with the docking/fusion complex in presynaptic terminals. Biochem. Biophys. Res. Commun. 213, 1107–1114 (1995).

5. Trimbuch, T. & Rosenmund, C. Should I stop or should I go? The role of complexin in neurotransmitter release. Nat. Rev. Neurosci. 17, 118–125 (2016).

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