JBC

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


     

Originally published In Press as doi:10.1074/jbc.M203229200 on June 6, 2002

J. Biol. Chem., Vol. 277, Issue 33, 30144-30152, August 16, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/33/30144    most recent
M203229200v1
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 Faisal, A.
Right arrow Articles by Nagamine, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Faisal, A.
Right arrow Articles by Nagamine, Y.
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?

Serine/Threonine Phosphorylation of ShcA
REGULATION OF PROTEIN-TYROSINE PHOSPHATASE-PEST BINDING AND INVOLVEMENT IN INSULIN SIGNALING*

Amir FaisalDagger , Mahmoud El-ShemerlyDagger §, Daniel Hess, and Yoshikuni Nagamine

From the Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058 Basel, Switzerland

Serine phosphorylation of the ShcA signaling molecule has been reported recently. In this work, we have identified 12-O-tetradecanoylphorbol-13-acetate (TPA)- and growth factor-induced serine/threonine phosphorylation sites in p52Shc and p66Shc. Among them, Ser29 in p52Shc (equivalent to Ser138 in p66Shc) was phosphorylated only after TPA stimulation. Phosphorylation of this site together with the intact phosphotyrosine-binding domain was essential for ShcA binding to the protein-tyrosine phosphatase PTP-PEST. TPA-induced ShcA phosphorylation at this site (and hence, its association with PTP-PEST) was inhibited by a protein kinase C-specific inhibitor and was induced by overexpression of constitutively active mutants of protein kinase Calpha , -epsilon , and -delta isoforms. Insulin also induced ShcA/PTP-PEST association, although to a lesser extent than TPA. Overexpression of a PTP-PEST binding-defective mutant of p52Shc (S29A) enhanced insulin-induced ERK activation in insulin receptor-overexpressing HIRc-B cells. Consistent with this, p52Shc S29A was more tyrosine-phosphorylated than wild-type p52Shc after insulin stimulation. Thus, we have identified a new mechanism whereby serine phosphorylation of ShcA controls the ability of its phosphotyrosine-binding domain to bind PTP-PEST, which is responsible for the dephosphorylation and down-regulation of ShcA after insulin stimulation.

* 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 Both authors contributed equally to this work.

§ Present address: Dept. of Biology, Kyushu University Graduate School, Faculty of Sciences, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan.

To whom correspondence should be addressed. Tel.: 41-61-697-6669; Fax: 41-61-697-3976; E-mail: Nagamine@fmi.ch.

Copyright © 2002 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 BiochemHome page
M. Morita, H. Matsuzaki, T. Yamamoto, Y. Fukami, and U. Kikkawa
Epidermal Growth Factor Receptor Phosphorylates Protein Kinase C {delta} at Tyr332 to form a Trimeric Complex with p66Shc in the H2O2-stimulated Cells
J. Biochem., January 1, 2008; 143(1): 31 - 38.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Obreztchikova, H. Elouardighi, M. Ho, B. A. Wilson, Z. Gertsberg, and S. F. Steinberg
Distinct Signaling Functions for Shc Isoforms in the Heart
J. Biol. Chem., July 21, 2006; 281(29): 20197 - 20204.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
Y. Hu, X. Wang, L. Zeng, D.-Y. Cai, K. Sabapathy, S. P. Goff, E. J. Firpo, and B. Li
ERK Phosphorylates p66shcA on Ser36 and Subsequently Regulates p27kip1 Expression via the Akt-FOXO3a Pathway: Implication of p27kip1 in Cell Response to Oxidative Stress
Mol. Biol. Cell, August 1, 2005; 16(8): 3705 - 3718.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. Audero, I. Cascone, F. Maniero, L. Napione, M. Arese, L. Lanfrancone, and F. Bussolino
Adaptor ShcA Protein Binds Tyrosine Kinase Tie2 Receptor and Regulates Migration and Sprouting but Not Survival of Endothelial Cells
J. Biol. Chem., March 26, 2004; 279(13): 13224 - 13233.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Faisal, S. Kleiner, and Y. Nagamine
Non-redundant Role of Shc in Erk Activation by Cytoskeletal Reorganization
J. Biol. Chem., January 30, 2004; 279(5): 3202 - 3211.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Ventura, M. Maccarana, V. A. Raker, and P. G. Pelicci
A Cryptic Targeting Signal Induces Isoform-specific Localization of p46Shc to Mitochondria
J. Biol. Chem., January 16, 2004; 279(3): 2299 - 2306.
[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 © 2002 by the American Society for Biochemistry and Molecular Biology.