Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 19, Issue 5, Pages 1825-1836Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E07-08-0781
Keywords
-
Categories
Funding
- Ministry of Education, Science, Sports and Culture of Japan [17048030, 18370081, 18050036, 18570186, 18657044]
- Medical Research Council [G117/554] Funding Source: researchfish
- MRC [G117/554] Funding Source: UKRI
- Grants-in-Aid for Scientific Research [18657044, 17048030, 18370081, 18050036, 18570186] Funding Source: KAKEN
Ask authors/readers for more resources
Certain endoplasmic reticulum (ER)-associated degradation (ERAD) substrates with transmembrane domains are segregated from other ER proteins and sorted into a juxtanuclear subcompartment, known as the ER quality control compartment. Bap31 is an ER protein with three transmembrane domains, and it is assumed to be a cargo receptor for ER export of some transmembrane proteins, especially those prone to ERAD. Here, we show that Bap31 is a component of the ER quality control compartment and that it moves between the peripheral ER and a juxtanuclear ER or ER-related compartment distinct from the conventional ER-Golgi intermediate compartment. The third and second transmembrane domains of Bap31 are principally responsible for the movement to and recycling from the juxtanuclear region, respectively. This cycling was blocked by depolymerization of microtubules and disruption of dynein-dynactin function. Overexpression of Sar1p and Arf1 mutants affected Bap31 cycling, suggesting that this cycling pathway is related to the conventional vesicular transport pathways.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available