Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality control.

ABSTRACT: In the endoplasmic reticulum (ER), most newly synthesized proteins are retained by quality control mechanisms until folded. Misfolded molecules are sorted to ER-associated degradation (ERAD) pathways for disposal. Reports of mutant proteins degraded in the vacuole/lysosome suggested an independent Golgi-based mechanism also at work. Although little is understood of the post-ER pathway, the growing number of variants using it suggests a major role in quality control. Why seemingly redundant mechanisms in sequential compartments are needed is unclear. To understand their physiological relationship, the identification of endogenous pathway-specific substrates is a prerequisite. With ERAD substrates already well characterized, the discovery of Wsc1p as an obligate substrate of Golgi quality co

SUBMITTER: Wang S 

PROVIDER: S-EPMC2847520 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature