JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M007573200 on February 5, 2001

J. Biol. Chem., Vol. 276, Issue 20, 16601-16610, May 18, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/20/16601    most recent
M007573200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pizzinat, N.
Right arrow Articles by Lanier, S. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pizzinat, N.
Right arrow Articles by Lanier, S. M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Identification of a Truncated Form of the G-protein Regulator AGS3 in Heart That Lacks the Tetratricopeptide Repeat Domains*

Nathalie PizzinatDagger , Aya Takesono§, and Stephen M. Lanier

From the Department of Pharmacology, Medical University of South Carolina, Charleston, South Carolina 29425

AGS3, a 650-amino acid protein encoded by an ~4-kilobase (kb) mRNA enriched in rat brain, is a Galpha i/Galpha t-binding protein that competes with Gbeta gamma for interaction with Galpha GDP and acts as a guanine nucleotide dissociation inhibitor for heterotrimeric G-proteins. An ~2-kb AGS3 mRNA (AGS3-SHORT) is enriched in rat and human heart. We characterized the heart-enriched mRNA, identified the encoded protein, and determined its ability to interact with and regulate the guanine nucleotide-binding properties of G-proteins. Screening of a rat heart cDNA library, 5'-rapid amplification of cDNA ends, and RNase protection assays identified two populations of cDNAs (1979 and 2134 nucleotides plus the polyadenylation site) that diverged from the larger 4-kb mRNA (AGS3-LONG) in the middle of the protein coding region. Transfection of COS-7 cells with AGS3-SHORT cDNAs resulted in the expression of a major immunoreactive AGS3 polypeptide (Mr ~ 23,000) with a translational start site at Met495 of AGS3-LONG. Immunoblots indicated the expression of the Mr ~ 23,000 polypeptide in rat heart. Glutathione S-transferase-AGS3-SHORT selectively interacted with the GDP-bound versus guanosine 5'-O-(3-thiotriphosphate) (GTPgamma S)-bound conformation of Galpha i2 and inhibited GTPgamma S binding to Galpha i2. Protein interaction assays with glutathione S-transferase-AGS3-SHORT and heart lysates indicated interaction of AGS3-SHORT with Galpha i1/2 and Galpha i3, but not Galpha s or Galpha q. Immunofluorescent imaging and subcellular fractionation following transient expression of AGS3-SHORT and AGS3-LONG in COS-7 and Chinese hamster ovary cells indicated distinct subcellular distributions of the two forms of AGS3. Thus, AGS3 exists as a short and long form, both of which apparently stabilize the GDP-bound conformation of Galpha i, but which differ in their tissue distribution and trafficking within the cell.

* This work was supported in part by National Institutes of Health Grants NS24821 and MH59931 (to S. M. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipient of a Medical University of South Carolina Health Sciences Foundation research fellowship and an Association de Recherche Contre le Cancer postdoctoral fellowship.

§ Supported in part by an Ikuei-Kai scholarship and a visiting graduate student from the Department of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan.

To whom correspondence should be addressed: Dept. of Pharmacology, Louisiana State University Health Sciences Center, 1901 Perdido St., New Orleans, LA 70112. Tel.: 504-568-4740; Fax: 504-568-2361; E-mail:slanie@lsuhsc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
N. An, J. B. Blumer, M. L. Bernard, and S. M. Lanier
The PDZ and Band 4.1 Containing Protein Frmpd1 Regulates the Subcellular Location of Activator of G-protein Signaling 3 and Its Interaction with G-proteins
J. Biol. Chem., September 5, 2008; 283(36): 24718 - 24728.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. J. Thomas, G. G. Tall, A. Adhikari, and S. R. Sprang
Ric-8A Catalyzes Guanine Nucleotide Exchange on G{alpha}i1 Bound to the GPR/GoLoco Exchange Inhibitor AGS3
J. Biol. Chem., August 22, 2008; 283(34): 23150 - 23160.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
J. B. Blumer, K. Lord, T. L. Saunders, A. Pacchioni, C. Black, E. Lazartigues, K. J. Varner, T. W. Gettys, and S. M. Lanier
Activator of G Protein Signaling 3 Null Mice: I. Unexpected Alterations in Metabolic and Cardiovascular Function
Endocrinology, August 1, 2008; 149(8): 3842 - 3849.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
B. Groves, Q. Gong, Z. Xu, C. Huntsman, C. Nguyen, D. Li, and D. Ma
A specific role of AGS3 in the surface expression of plasma membrane proteins
PNAS, November 13, 2007; 104(46): 18103 - 18108.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
C. Marty, T. Kozasa, M. T. Quinn, and R. D. Ye
Activation State-Dependent Interaction between G{alpha}i and p67phox.
Mol. Cell. Biol., July 1, 2006; 26(13): 5190 - 5200.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Yasumi, T. Sakisaka, T. Hoshino, T. Kimura, Y. Sakamoto, T. Yamanaka, S. Ohno, and Y. Takai
Direct Binding of Lgl2 to LGN during Mitosis and Its Requirement for Normal Cell Division
J. Biol. Chem., February 25, 2005; 280(8): 6761 - 6765.
[Abstract] [Full Text] [PDF]

Home page
 IOVSHome page
K. S. Nair, A. Mendez, J. B. Blumer, D. H. Rosenzweig, and V. Z. Slepak
The Presence of a Leu-Gly-Asn Repeat-Enriched Protein (LGN), a Putative Binding Partner of Transducin, in ROD Photoreceptors
Invest. Ophthalmol. Vis. Sci., January 1, 2005; 46(1): 383 - 389.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
X. Cao, M. J. Cismowski, M. Sato, J. B. Blumer, and S. M. Lanier
Identification and Characterization of AGS4: A PROTEIN CONTAINING THREE G-PROTEIN REGULATORY MOTIFS THAT REGULATE THE ACTIVATION STATE OF Gi{alpha}
J. Biol. Chem., June 25, 2004; 279(26): 27567 - 27574.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Sato, T. W. Gettys, and S. M. Lanier
AGS3 and Signal Integration by G{alpha}s- and G{alpha}i-coupled Receptors: AGS3 BLOCKS THE SENSITIZATION OF ADENYLYL CYCLASE FOLLOWING PROLONGED STIMULATION OF A G{alpha}i-COUPLED RECEPTOR BY INFLUENCING PROCESSING OF G{alpha}i
J. Biol. Chem., April 2, 2004; 279(14): 13375 - 13382.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Adhikari and S. R. Sprang
Thermodynamic Characterization of the Binding of Activator of G Protein Signaling 3 (AGS3) and Peptides Derived from AGS3 with G{alpha}i1
J. Biol. Chem., December 19, 2003; 278(51): 51825 - 51832.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
R. Kaushik, F. Yu, W. Chia, X. Yang, and S. Bahri
Subcellular Localization of LGN During Mitosis: Evidence for Its Cortical Localization in Mitotic Cell Culture Systems and Its Requirement for Normal Cell Cycle Progression
Mol. Biol. Cell, August 1, 2003; 14(8): 3144 - 3155.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. B. Blumer, M. L. Bernard, Y. K. Peterson, J.-i. Nezu, P. Chung, D. J. Dunican, J. A. Knoblich, and S. M. Lanier
Interaction of Activator of G-protein Signaling 3 (AGS3) with LKB1, a Serine/Threonine Kinase Involved in Cell Polarity and Cell Cycle Progression: PHOSPHORYLATION OF THE G-PROTEIN REGULATORY (GPR) MOTIF AS A REGULATORY MECHANISM FOR THE INTERACTION OF GPR MOTIFS WITH Gi{alpha}
J. Biol. Chem., June 20, 2003; 278(26): 23217 - 23220.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Pattingre, L. De Vries, C. Bauvy, I. Chantret, F. Cluzeaud, E. Ogier-Denis, A. Vandewalle, and P. Codogno
The G-protein Regulator AGS3 Controls an Early Event during Macroautophagy in Human Intestinal HT-29 Cells
J. Biol. Chem., May 30, 2003; 278(23): 20995 - 21002.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. B. Blumer, L. J. Chandler, and S. M. Lanier
Expression Analysis and Subcellular Distribution of the Two G-protein Regulators AGS3 and LGN Indicate Distinct Functionality. LOCALIZATION OF LGN TO THE MIDBODY DURING CYTOKINESIS
J. Biol. Chem., May 3, 2002; 277(18): 15897 - 15903.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. K. Peterson, S. Hazard III, S. G. Graber, and S. M. Lanier
Identification of Structural Features in the G-protein Regulatory Motif Required for Regulation of Heterotrimeric G-proteins
J. Biol. Chem., February 22, 2002; 277(9): 6767 - 6770.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.