Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo
Zippering of SNARE complexes spanning docked membranes is essential for most intracellular fusion events. Here, we explore how SNARE regulators operate on discrete zippering states. The formation of a metastable trans-complex, catalyzed by HOPS and its SM subunit Vps33, is followed by subsequent zip...
Main Authors: | Matthew L Schwartz, Daniel P Nickerson, Braden T Lobingier, Rachael L Plemel, Mengtong Duan, Cortney G Angers, Michael Zick, Alexey J Merz |
---|---|
Format: | Article |
Language: | English |
Published: |
eLife Sciences Publications Ltd
2017-09-01
|
Series: | eLife |
Subjects: | |
Online Access: | https://elifesciences.org/articles/27396 |
Similar Items
-
Identification and Characterization of the Interaction between VPS33B and SNAREs
by: Puhacz, Michael
Published: (2011) -
Identification and Characterization of the Interaction between VPS33B and SNAREs
by: Puhacz, Michael
Published: (2011) -
The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation
by: Travis J Eisemann, et al.
Published: (2020-08-01) -
Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering
by: Hongki Song, et al.
Published: (2021-05-01) -
Multiple factors maintain assembled trans-SNARE complexes in the presence of NSF and αSNAP
by: Eric A Prinslow, et al.
Published: (2019-01-01)