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

J. Biol. Chem., Vol. 276, Issue 3, 2007-2014, January 19, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/3/2007    most recent M003527200v1 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 Guillard, C. Articles by Duprez, V. Search for Related Content PubMed PubMed Citation Articles by Guillard, C. Articles by Duprez, V. Social Bookmarking                      What's this?

Coupling of Heterotrimeric G_i Proteins to the Erythropoietin Receptor^*

Christine Guillard, Stany Chrétien, Ralf Jockers^§, Serge Fichelson, Patrick Mayeux, and Véronique Duprez^¶

From the  INSERM, U 363 and ^§ CNRS-UPR 0415, Institut Cochin de Génétique Moléculaire, 75014 Paris, France

To identify new proteins involved in erythropoietin (Epo) signal transduction, we purified the entire set of proteins reactive with anti-phosphotyrosine antibodies from Epo-stimulated UT7 cells. Antisera generated against these proteins were used to screen a EXlox expression library. One of the isolated cDNAs encodes G_2, the ₂ subunit of heterotrimeric GTP-binding proteins. G and G_i coprecipitated with the Epo receptor (EpoR) in extracts from human and murine cell lines and from normal human erythroid progenitor cells. In addition, in vitro G associated with a fusion protein containing the intracellular domain of the EpoR. Using EpoR mutants, we found that the distal part of the EpoR (between amino acids 459-479) was required for G_i binding. Epo activation of these cells induced the release of the G_i protein from the EpoR. Moreover in isolated cell membranes, Epo treatment inhibited ADP-ribosylation of G_i and increased the binding of GTP. Our results show that heterotrimeric G_i proteins associate with the C-terminal end of the EpoR. Receptor activation leads to the activation and dissociation of G_i from the receptor, suggesting a functional role of G_i protein in Epo signal transduction.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				A. W. Orr, C. E. Pedraza, M. A. Pallero, C. A. Elzie, S. Goicoechea, D. K. Strickland, and J. E. Murphy-Ullrich Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly J. Cell Biol., June 23, 2003; 161(6): 1179 - 1189. [Abstract] [Full Text] [PDF]

				C. Guillard, S. Chretien, A.-S. Pelus, F. Porteu, O. Muller, P. Mayeux, and V. Duprez Activation of the Mitogen-activated Protein Kinases Erk1/2 by Erythropoietin Receptor via a Gi Protein beta gamma -Subunit-initiated Pathway J. Biol. Chem., March 21, 2003; 278(13): 11050 - 11056. [Abstract] [Full Text] [PDF]

				P. Talbot, B. D. Shur, and D. G. Myles Cell Adhesion and Fertilization: Steps in Oocyte Transport, Sperm-Zona Pellucida Interactions, and Sperm-Egg Fusion Biol Reprod, January 1, 2003; 68(1): 1 - 9. [Abstract] [Full Text] [PDF]

				C. Meunier, D. Bordereaux, F. Porteu, S. Gisselbrecht, S. Chretien, and G. Courtois Cloning and Characterization of a Family of Proteins Associated with Mpl J. Biol. Chem., March 8, 2002; 277(11): 9139 - 9147. [Abstract] [Full Text] [PDF]