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J. Biol. Chem., Vol. 275, Issue 28, 21331-21339, July 14, 2000

This Article Full Text Full Text (PDF) All Versions of this Article: 275/28/21331    most recent M909642199v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Vitale, N. Articles by Vaughan, M. Search for Related Content PubMed PubMed Citation Articles by Vitale, N. Articles by Vaughan, M. Social Bookmarking                      What's this?

Specific Functional Interaction of Human Cytohesin-1 and ADP-ribosylation Factor Domain Protein (ARD1)^*

Nicolas Vitale^§, Gustavo Pacheco-Rodriguez^¶, Victor J. Ferrans, William Riemenschneider, Joel Moss, and Martha Vaughan

From the Pulmonary-Critical Care Medicine Branch and the  Pathology Section, NHLBI, National Institutes of Health, Bethesda, Maryland 20892

Activation of ADP-ribosylation factors (ARFs) is mediated by guanine nucleotide-exchange proteins, which accelerate conversion of inactive ARF-GDP to active ARF-GTP. ARF domain protein (ARD1), a 64-kDa GTPase with a C-terminal ADP-ribosylation factor domain, is localized to lysosomes and the Golgi apparatus. When ARD1 was used as bait to screen a human liver cDNA library using the yeast two-hybrid system, a cDNA for cytohesin-1, a ~50-kDa protein with ARF guanine nucleotide-exchange protein activity, was isolated. In this system, ARD1-GDP interacted well with cytohesin-1 but very poorly with cytohesin-2. In agreement, cytohesin-1, but not cytohesin-2, markedly accelerated [³⁵S]guanosine 5'-3-O-(thio)triphosphate binding to ARD1. The effector region of the ARF domain of ARD1 appeared to be critical for the specific interaction with cytohesin-1. Replacement of single amino acids in the Sec7 domains of cytohesin-1 and -2 showed that residue 30 is critical for specificity. In transfected COS-7 cells, overexpressed ARD1 and cytohesin-1 were partially colocalized, as determined by confocal fluorescence microscopy. It was concluded that cytohesin-1 is likely to be involved in ARD1 activation, consistent with a role for ARD1 in the regulation of vesicular trafficking.

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