HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 8, 7105-7111, February 20, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/8/7105    most recent M311702200v1 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 Shiba, Y. Articles by Nakayama, K. Search for Related Content PubMed PubMed Citation Articles by Shiba, Y. Articles by Nakayama, K. Social Bookmarking                      What's this?

GAT (GGA and Tom1) Domain Responsible for Ubiquitin Binding and Ubiquitination^*

Yoko Shiba¶||, Yohei Katoh||, Tomoo Shiba**, Kaori Yoshino||, Hiroyuki Takatsu, Hiromi Kobayashi, Hye-Won Shin, Soichi Wakatsuki**, and Kazuhisa Nakayama||¶¶

From the Institute of Biological Sciences, University of Tsukuba, Tsukuba, Ibaraki 305-8572, Japan, Faculty of Pharmaceutical Sciences and Cancer Research Institute, Kanazawa University, Kanazawa, Ishikawa 920-0934, Japan, ^**Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki 305-0801, Japan, and RIKEN Research Center for Allergy and Immunology (RCAI), Yokohama, Kanagawa 230-0045, Japan

GGAs (Golgi-localizing, -adaptin ear domain homology, ADP-ribosylation factor (ARF)-binding proteins) are a family of monomeric adaptor proteins involved in membrane trafficking from the trans-Golgi network to endosomes. The GAT (GGA and Tom1) domains of GGAs have previously been shown to interact with GTP-bound ARF and to be crucial for membrane recruitment of GGAs. Here we show that the C-terminal subdomain of the GAT domain, which is distinct from the N-terminal GAT subdomain responsible for ARF binding, can bind ubiquitin. The binding is mediated by interactions between residues on one side of the 3 helix of the GAT domain and those on the so-called Ile-44 surface patch of ubiquitin. The binding of the GAT domain to ubiquitin can be enhanced by the presence of a GTP-bound form of ARF. Furthermore, GGA itself is ubiquitinated in a manner dependent on the GAT-ubiquitin interaction. These results delineate the molecular basis for the interaction between ubiquitin and GAT and suggest that GGA-mediated trafficking is regulated by the ubiquitin system as endosomal trafficking mediated by other ubiquitin-binding proteins.

Received for publication, October 24, 2003 , and in revised form, November 26, 2003.

^* This work was supported in part by grants from the Japan Society for Promotion of Science, from the Ministry of Education, Culture, Sports, Science and Technology of Japan, from the Protein 3000 Project, and from the Naito Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Recipient of a fellowship from the Japan Society for Promotion of Science for Japanese Junior Scientists.

^|| Present address: Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.

^¶¶ To whom correspondence should be addressed: Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. Tel.: 81-75-753-4527; Fax: 81-75-753-4557; E-mail: kazunaka{at}pharm.kyoto-u.ac.jp.

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

This article has been cited by other articles:

				J. Wang, H.-Q. Sun, E. Macia, T. Kirchhausen, H. Watson, J. S. Bonifacino, and H. L. Yin PI4P Promotes the Recruitment of the GGA Adaptor Proteins to the Trans-Golgi Network and Regulates Their Recognition of the Ubiquitin Sorting Signal Mol. Biol. Cell, July 1, 2007; 18(7): 2646 - 2655. [Abstract] [Full Text] [PDF]

				Y. Pak, W. K. Glowacka, M. C. Bruce, N. Pham, and D. Rotin Transport of LAPTM5 to lysosomes requires association with the ubiquitin ligase Nedd4, but not LAPTM5 ubiquitination J. Cell Biol., November 20, 2006; 175(4): 631 - 645. [Abstract] [Full Text] [PDF]

				C. A. F. von Arnim, R. Spoelgen, I. D. Peltan, M. Deng, S. Courchesne, M. Koker, T. Matsui, H. Kowa, S. F. Lichtenthaler, M. C. Irizarry, et al. GGA1 Acts as a Spatial Switch Altering Amyloid Precursor Protein Trafficking and Processing J. Neurosci., September 27, 2006; 26(39): 9913 - 9922. [Abstract] [Full Text] [PDF]

				G. Costaguta, M. C. Duncan, G. E. Fernandez, G. H. Huang, and G. S. Payne Distinct Roles for TGN/Endosome Epsin-like Adaptors Ent3p and Ent5p Mol. Biol. Cell, September 1, 2006; 17(9): 3907 - 3920. [Abstract] [Full Text] [PDF]

				O. Staub and D. Rotin Role of Ubiquitylation in Cellular Membrane Transport Physiol Rev, April 1, 2006; 86(2): 669 - 707. [Abstract] [Full Text] [PDF]

				R. Mattera, Y. C. Tsai, A. M. Weissman, and J. S. Bonifacino The Rab5 Guanine Nucleotide Exchange Factor Rabex-5 Binds Ubiquitin (Ub) and Functions as a Ub Ligase through an Atypical Ub-interacting Motif and a Zinc Finger Domain J. Biol. Chem., March 10, 2006; 281(10): 6874 - 6883. [Abstract] [Full Text] [PDF]

				S. Kametaka, R. Mattera, and J. S. Bonifacino Epidermal Growth Factor-Dependent Phosphorylation of the GGA3 Adaptor Protein Regulates Its Recruitment to Membranes Mol. Cell. Biol., September 15, 2005; 25(18): 7988 - 8000. [Abstract] [Full Text] [PDF]

				M. Kawasaki, T. Shiba, Y. Shiba, Y. Yamaguchi, N. Matsugaki, N. Igarashi, M. Suzuki, R. Kato, K. Kato, K. Nakayama, et al. Molecular mechanism of ubiquitin recognition by GGA3 GAT domain Genes Cells, July 1, 2005; 10(7): 639 - 654. [Abstract] [Full Text] [PDF]

				R. Puertollano Interactions of TOM1L1 with the Multivesicular Body Sorting Machinery J. Biol. Chem., March 11, 2005; 280(10): 9258 - 9264. [Abstract] [Full Text] [PDF]

				W. Li, C. Marshall, L. Mei, L. Dzubow, C. Schmults, M. Dans, and J. Seykora Srcasm Modulates EGF and Src-kinase Signaling in Keratinocytes J. Biol. Chem., February 18, 2005; 280(7): 6036 - 6046. [Abstract] [Full Text] [PDF]

				G. Prag, S. Lee, R. Mattera, C. N. Arighi, B. M. Beach, J. S. Bonifacino, and J. H. Hurley Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, {gamma}-ear-containing, ADP-ribosylation-factor-binding proteins PNAS, February 15, 2005; 102(7): 2334 - 2339. [Abstract] [Full Text] [PDF]

				P. S. Bilodeau, S. C. Winistorfer, M. M. Allaman, K. Surendhran, W. R. Kearney, A. D. Robertson, and R. C. Piper The GAT Domains of Clathrin-associated GGA Proteins Have Two Ubiquitin Binding Motifs J. Biol. Chem., December 24, 2004; 279(52): 54808 - 54816. [Abstract] [Full Text] [PDF]

				J. Kzhyshkowska, A. Gratchev, J.-H. Martens, O. Pervushina, S. Mamidi, S. Johansson, K. Schledzewski, B. Hansen, X. He, J. Tang, et al. Stabilin-1 localizes to endosomes and the trans-Golgi network in human macrophages and interacts with GGA adaptors J. Leukoc. Biol., December 1, 2004; 76(6): 1151 - 1161. [Abstract] [Full Text] [PDF]

				E. Stang, F. D. Blystad, M. Kazazic, V. Bertelsen, T. Brodahl, C. Raiborg, H. Stenmark, and I. H. Madshus Cbl-dependent Ubiquitination Is Required for Progression of EGF Receptors into Clathrin-coated Pits Mol. Biol. Cell, August 1, 2004; 15(8): 3591 - 3604. [Abstract] [Full Text] [PDF]

				R. Mattera, R. Puertollano, W. J. Smith, and J. S. Bonifacino The Trihelical Bundle Subdomain of the GGA Proteins Interacts with Multiple Partners through Overlapping but Distinct Sites J. Biol. Chem., July 23, 2004; 279(30): 31409 - 31418. [Abstract] [Full Text] [PDF]

				Y. Katoh, Y. Shiba, H. Mitsuhashi, Y. Yanagida, H. Takatsu, and K. Nakayama Tollip and Tom1 Form a Complex and Recruit Ubiquitin-conjugated Proteins onto Early Endosomes J. Biol. Chem., June 4, 2004; 279(23): 24435 - 24443. [Abstract] [Full Text] [PDF]