Grp1-associated scaffold protein (GRASP) is a regulator of the ADP ribosylation factor 6 (Arf6)-dependent membrane trafficking pathway

Anand Venkataraman, Daniel J. Nevrivy, Theresa M. Filtz, Mark Leid

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1115-1128
Number of pages14
JournalCell biology international
Issue number12
StatePublished - Dec 1 2012
Externally publishedYes


  • Arf6
  • Clathrin-independent
  • Receptor-recycling
  • Scaffold protein
  • Trafficking

ASJC Scopus subject areas

  • Cell Biology


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