TY - JOUR
T1 - The machinery of vesicle fusion
AU - Stanton, Abigail E.
AU - Hughson, Frederick M.
N1 - Funding Information: We thank Mary Munson, Jose Rizo, Bill Wickner, Yongli Zhang, and members of the Hughson laboratory past and present for helpful advice and discussion. This work was supported by National Institutes of Health grants T32GM007388 (AES) and R01GM071574 (FMH). Publisher Copyright: © 2023 Elsevier Ltd
PY - 2023/8
Y1 - 2023/8
N2 - The compartmentalization of eukaryotic cells is reliant on the fidelity of vesicle-mediated intracellular transport. Vesicles deliver their cargo via membrane fusion, a process requiring membrane tethers, Sec1/Munc18 (SM) proteins, and SNAREs. These components function in concert to ensure that membrane fusion is efficient and accurate, but the mechanisms underlying their cooperative action are still in many respects mysterious. In this brief review, we highlight recent progress toward a more integrative understanding of the vesicle fusion machinery. We focus particular attention on cryo-electron microscopy structures of intact multisubunit tethers in complex with SNAREs or SM proteins, as well as a structure of an SM protein bound to multiple SNAREs. The insights gained from this work emphasize the advantages of studying the fusion machinery intact and in context.
AB - The compartmentalization of eukaryotic cells is reliant on the fidelity of vesicle-mediated intracellular transport. Vesicles deliver their cargo via membrane fusion, a process requiring membrane tethers, Sec1/Munc18 (SM) proteins, and SNAREs. These components function in concert to ensure that membrane fusion is efficient and accurate, but the mechanisms underlying their cooperative action are still in many respects mysterious. In this brief review, we highlight recent progress toward a more integrative understanding of the vesicle fusion machinery. We focus particular attention on cryo-electron microscopy structures of intact multisubunit tethers in complex with SNAREs or SM proteins, as well as a structure of an SM protein bound to multiple SNAREs. The insights gained from this work emphasize the advantages of studying the fusion machinery intact and in context.
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U2 - https://doi.org/10.1016/j.ceb.2023.102191
DO - https://doi.org/10.1016/j.ceb.2023.102191
M3 - Review article
C2 - 37421936
SN - 0955-0674
VL - 83
JO - Current Opinion in Cell Biology
JF - Current Opinion in Cell Biology
M1 - 102191
ER -