Back to Search
Start Over
SNARE chaperone Sly1 directly mediates close-range vesicle tethering.
- Source :
-
Journal of Cell Biology . 6/3/2024, Vol. 223 Issue 6, p1-S4. 23p. - Publication Year :
- 2024
-
Abstract
- The essential Golgi protein Sly1 is a member of the Sec1/mammalian Unc-18 (SM) family of SNARE chaperones. Sly1 was originally identified through remarkable gain-of-function alleles that bypass requirements for diverse vesicle tethering factors. Employing genetic analyses and chemically defined reconstitutions of ER-Golgi fusion, we discovered that a loop conserved among Sly1 family members is not only autoinhibitory but also acts as a positive effector. An amphipathic lipid packing sensor (ALPS)-like helix within the loop directly binds high-curvature membranes. Membrane binding is required for relief of Sly1 autoinhibition and also allows Sly1 to directly tether incoming vesicles to the Qa-SNARE on the target organelle. The SLY1-20 mutation bypasses requirements for diverse tethering factors but loses this ability if the tethering activity is impaired. We propose that long-range tethers, including Golgins and multisubunit tethering complexes, hand off vesicles to Sly1, which then tethers at close range to initiate trans-SNARE complex assembly and fusion in the early secretory pathway. [ABSTRACT FROM AUTHOR]
- Subjects :
- *ALLELES
*LIPIDS
*DETECTORS
*PROTEINS
*FAMILIES
*COATED vesicles
Subjects
Details
- Language :
- English
- ISSN :
- 00219525
- Volume :
- 223
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- Journal of Cell Biology
- Publication Type :
- Academic Journal
- Accession number :
- 177768562
- Full Text :
- https://doi.org/10.1083/jcb.202001032