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- Title
Grp1-associated scaffold protein (GRASP) is a regulator of the ADP ribosylation factor 6 (Arf6)-dependent membrane trafficking pathway.
- Authors
Venkataraman, Anand; Nevrivy, Daniel J.; Filtz, Theresa M.; Leid, Mark
- Abstract
GRASP interacts with Grp1 ( general receptor for phosphoinositides 1; cytohesin 3), which catalyses nucleotide exchange on and activation of Arf6 (ADP-ribosylation factor-6). Arf6 is a low-molecular-mass GTPase that regulates key aspects of endocytic recycling pathways. Overexpressed GRASP accumulated in the juxtanuclear ERC (endocytic recycling compartment). GRASP co-localized with a constitutively inactive mutant of Arf6 in the ERC such that it was reversed by expression of wild-type Grp1. Co-expression of GRASP and Grp1 promoted membrane ruffling, a cellular hallmark of Arf6 activation. GRASP accumulation in ERC was found to block recycling of the MHC-I (major histocompatibility complex-I), which is trafficked by the Arf6-dependent pathway. In contrast, overexpression of GRASP had no effect on the recycling of transferrin receptors, which are trafficked by a clathrin-dependent pathway. The findings suggest that GRASP regulates the non-clathrin/Arf6-dependent, plasma membrane recycling and signalling pathways.
- Subjects
ADP-ribosylation factors; CELL receptors; GUANOSINE triphosphatase; GENE expression; MAJOR histocompatibility complex; CLATHRIN; CELLULAR signal transduction
- Publication
Cell Biology International, 2012, Vol 36, Issue 12, p1115
- ISSN
1065-6995
- Publication type
Article
- DOI
10.1042/CBI20120221