Abstract
Eukaryotic secretory proteins exit the endoplasmic reticulum (ER) via transport vesicles generated by
the essential coat protein complex II (COPII) proteins. The outer coat complex, Sec13-Sec31,
forms a scaffold that is thought to enforce curvature. By exploiting yeast bypass-of-sec-thirteen (bst)
mutants, where Sec13p is dispensable, we probed the relationship between a compromised COPII
coat and the cellular context in which it could still function. Genetic and biochemical analyses
suggested that Sec13p was required to generate vesicles from membranes that contained asymmetrically
distributed cargoes that were likely to confer opposing curvature. Thus, Sec13p may rigidify the
COPII cage and increase its membrane-bending capacity; this function could be bypassed when a bst
mutation renders the membrane more deformable.
the essential coat protein complex II (COPII) proteins. The outer coat complex, Sec13-Sec31,
forms a scaffold that is thought to enforce curvature. By exploiting yeast bypass-of-sec-thirteen (bst)
mutants, where Sec13p is dispensable, we probed the relationship between a compromised COPII
coat and the cellular context in which it could still function. Genetic and biochemical analyses
suggested that Sec13p was required to generate vesicles from membranes that contained asymmetrically
distributed cargoes that were likely to confer opposing curvature. Thus, Sec13p may rigidify the
COPII cage and increase its membrane-bending capacity; this function could be bypassed when a bst
mutation renders the membrane more deformable.
| Original language | English |
|---|---|
| Pages (from-to) | 1359-1362 |
| Number of pages | 4 |
| Journal | Science |
| Volume | 335 |
| Issue number | 6074 |
| Early online date | 2 Feb 2012 |
| DOIs | |
| Publication status | Published - 16 Mar 2012 |