Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Bap31 is an itinerant protein that moves between the peripheral ER and a juxtanuclear compartment related to ER-associated degradation

Wakana, Yuichi, Takai, Sawako, Nakajima, Ken-ichi, Tani, Katsuko, Yamamoto, Akitsugu, Watson, Peter Duncan ORCID: https://orcid.org/0000-0003-0250-7852, Stephens, David J., Hauri, Hans-Peter and Tagaya, Mitsuo 2008. Bap31 is an itinerant protein that moves between the peripheral ER and a juxtanuclear compartment related to ER-associated degradation. Molecular Biology of the Cell 19 (5) , pp. 1825-1836. 10.1091/mbc.E07-08-0781

Full text not available from this repository.

Abstract

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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: American Society for Cell Biology
ISSN: 1059-1524
Last Modified: 25 Oct 2022 10:06
URI: https://orca.cardiff.ac.uk/id/eprint/61140

Citation Data

Cited 62 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item Edit Item