QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 30 May 2006
doi: 10.1242/jcs.02997

This Article Figures Only Full Text Full Text (PDF) Supplementary Material All Versions of this Article: jcs.02997v1 119/12/2604    most recent Alert me when this article is cited Alert me if a correction is posted 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 Yahara, N. Articles by Nakano, A. Search for Related Content PubMed PubMed Citation Articles by Yahara, N. Articles by Nakano, A. Social Bookmarking                         What's this?

The Arf1p GTPase-activating protein Glo3p executes its regulatory function through a conserved repeat motif at its C-terminus

N. Yahara^1,*, K. Sato^1,2 and A. Nakano^1,3,

¹ Molecular Membrane Biology Laboratory, RIKEN Discovery Research Institute, Hirosawa, Wako, Saitama 351-0198, Japan
² PRESTO, Japan Science and Technology Agency, Hirosawa, Wako, Saitama 351-0198, Japan
³ Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

Author for correspondence (e-mail: nakano{at}riken.jp)

Accepted 21 March 2006

ADP-ribosylation factors (Arfs), key regulators of intracellular membrane traffic, are known to exert multiple roles in vesicular transport. We previously isolated eight temperature-sensitive (ts) mutants of the yeast ARF1 gene, which showed allele-specific defects in protein transport, and classified them into three groups of intragenic complementation. In this study, we show that the overexpression of Glo3p, one of the GTPase-activating proteins of Arf1p (ArfGAP), suppresses the ts growth of a particular group of the arf1 mutants (arf1-16 and arf1-17). Other ArfGAPs do not show such a suppression activity. All these ArfGAPs show sequence similarity in the ArfGAP catalytic domain, but are divergent in the rest of molecules. By domain swapping analysis of Glo3p and another ArfGAP, Gcs1p, we have shown that the non-catalytic C-terminal region of Glo3p is required for the suppression of the growth defect in the arf1 ts mutants. Interestingly, Glo3p and its homologues from other eukaryotes harbor a well-conserved repeated ISSxxxFG sequence near the C-terminus, which is not found in Gcs1p and its homologues. We name this region the Glo3 motif and present evidence that the motif is required for the function of Glo3p in vivo.

Key words: ArfGAP, Glo3p, Glo3 motif

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				A. Saitoh, H.-W. Shin, A. Yamada, S. Waguri, and K. Nakayama Three Homologous ArfGAPs Participate in Coat Protein I-mediated Transport J. Biol. Chem., May 15, 2009; 284(20): 13948 - 13957. [Abstract] [Full Text] [PDF]

				L. Kliouchnikov, J. Bigay, B. Mesmin, A. Parnis, M. Rawet, N. Goldfeder, B. Antonny, and D. Cassel Discrete Determinants in ArfGAP2/3 Conferring Golgi Localization and Regulation by the COPI Coat Mol. Biol. Cell, February 1, 2009; 20(3): 859 - 869. [Abstract] [Full Text] [PDF]

				C. Weimer, R. Beck, P. Eckert, I. Reckmann, J. Moelleken, B. Brugger, and F. Wieland Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking J. Cell Biol., November 18, 2008; 183(4): 725 - 735. [Abstract] [Full Text] [PDF]

				A. Aguilera-Romero, J. Kaminska, A. Spang, H. Riezman, and M. Muniz The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus J. Cell Biol., February 25, 2008; 180(4): 713 - 720. [Abstract] [Full Text] [PDF]