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Grp1‐associated scaffold protein (GRASP) is a regulator of the ADP ribosylation factor 6 (Arf6)‐dependent membrane trafficking pathway
Author(s) -
Venkataraman Anand,
Nevrivy Daniel J.,
Filtz Theresa M.,
Leid Mark
Publication year - 2012
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1042/cbi20120221
Subject(s) - adp ribosylation factor , scaffold protein , microbiology and biotechnology , endocytic cycle , guanine nucleotide exchange factor , small gtpase , endosome , membrane ruffling , signal transducing adaptor protein , gtpase , biology , chemistry , signal transduction , receptor , endocytosis , golgi apparatus , biochemistry , cell , cytoskeleton , endoplasmic reticulum , intracellular
GRASP interacts with Grp1 ( g eneral r eceptor for p hosphoinositides 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.