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

J. Biol. Chem., Vol. 276, Issue 10, 7246-7257, March 9, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/10/7246    most recent M004389200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sekiguchi, T. Articles by Nishimoto, T. Search for Related Content PubMed PubMed Citation Articles by Sekiguchi, T. Articles by Nishimoto, T. Social Bookmarking                      What's this?

Novel G Proteins, Rag C and Rag D, Interact with GTP-binding Proteins, Rag A and Rag B^*

Takeshi Sekiguchi, Eiji Hirose, Nobutaka Nakashima, Miki Ii, and Takeharu Nishimoto

From the Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan

Rag A/Gtr1p are G proteins and are known to be involved in the RCC1-Ran pathway. We employed the two-hybrid method using Rag A as the bait to identify proteins binding to Rag A, and we isolated two novel human G proteins, Rag C and Rag D. Rag C demonstrates homology with Rag D (81.1% identity) and with Gtr2p of Saccharomyces cerevisiae (46.1% identity), and it belongs to the Rag A subfamily of the Ras family. Rag C and Rag D contain conserved GTP-binding motifs (PM-1, -2, and -3) in their N-terminal regions. Recombinant glutathione S-transferase fusion protein of Rag C efficiently bound to both [³H]GTP and [³H]GDP. Rag A was associated with both Rag C and Rag D in their C-terminal regions where a potential leucine zipper motif and a coiled-coil structure were found. Rag C and D were associated with both the GDP and GTP forms of Rag A. Both Rag C and Rag D changed their subcellular localization, depending on the nucleotide-bound state of Rag A. In a similar way, the disruption of S. cerevisiae GTR1 resulted in a change in the localization of Gtr2p.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF272035 and AF272036.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				J. Avruch, X. Long, S. Ortiz-Vega, J. Rapley, A. Papageorgiou, and N. Dai Amino acid regulation of TOR complex 1 Am J Physiol Endocrinol Metab, April 1, 2009; 296(4): E592 - E602. [Abstract] [Full Text] [PDF]

				Y. Sancak, T. R. Peterson, Y. D. Shaul, R. A. Lindquist, C. C. Thoreen, L. Bar-Peled, and D. M. Sabatini The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1 Science, June 13, 2008; 320(5882): 1496 - 1501. [Abstract] [Full Text] [PDF]

				T. Sekiguchi, T. Hayano, M. Yanagida, N. Takahashi, and T. Nishimoto NOP132 is required for proper nucleolus localization of DEAD-box RNA helicase DDX47 Nucleic Acids Res., September 11, 2006; 34(16): 4593 - 4608. [Abstract] [Full Text] [PDF]

				Y. Todaka, Y. Wang, K. Tashiro, N. Nakashima, T. Nishimoto, and T. Sekiguchi Association of the GTP-Binding Protein Gtr1p With Rpc19p, a Shared Subunit of RNA Polymerase I and III in Yeast Saccharomyces cerevisiae Genetics, August 1, 2005; 170(4): 1515 - 1524. [Abstract] [Full Text] [PDF]

				J. Colicelli Human RAS Superfamily Proteins and Related GTPases Sci. Signal., September 14, 2004; 2004(250): re13 - re13. [Abstract] [Full Text] [PDF]

				T. Sekiguchi, Y. Todaka, Y. Wang, E. Hirose, N. Nakashima, and T. Nishimoto A Novel Human Nucleolar Protein, Nop132, Binds to the G Proteins, RRAG A/C/D J. Biol. Chem., February 27, 2004; 279(9): 8343 - 8350. [Abstract] [Full Text] [PDF]

				T. Nakamura, M. Komiya, K. Sone, E. Hirose, N. Gotoh, H. Morii, Y. Ohta, and N. Mori Grit, a GTPase-Activating Protein for the Rho Family, Regulates Neurite Extension through Association with the TrkA Receptor and N-Shc and CrkL/Crk Adapter Molecules Mol. Cell. Biol., December 15, 2002; 22(24): 8721 - 8734. [Abstract] [Full Text] [PDF]