This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 E-mail 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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Standen, C. L.
Right arrow Articles by Davis, R. J.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Standen, C. L.
Right arrow Articles by Davis, R. J.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, September 2009, p. 4831-4840, Vol. 29, No. 17
0270-7306/09/$08.00+0     doi:10.1128/MCB.00155-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Signal Transduction Cross Talk Mediated by Jun N-Terminal Kinase-Interacting Protein and Insulin Receptor Substrate Scaffold Protein Complexes{triangledown}

Claire L. Standen,1 Norman J. Kennedy,1 Richard A. Flavell,2 and Roger J. Davis1*

Howard Hughes Medical Institute and Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605,1 Howard Hughes Medical Institute and Section of Immunobiology, Yale University School of Medicine, Yale University, New Haven, Connecticut 065202

Received 3 February 2009/ Returned for modification 16 March 2009/ Accepted 23 June 2009

Scaffold proteins have been established as important mediators of signal transduction specificity. The insulin receptor substrate (IRS) proteins represent a critical group of scaffold proteins that are required for signal transduction by the insulin receptor, including the activation of phosphatidylinositol 3 kinase. The c-Jun NH2-terminal kinase (JNK)-interacting proteins (JIPs) represent a different group of scaffold molecules that are implicated in the regulation of the JNK. These two signaling pathways are functionally linked because JNK can phosphorylate IRS1 on the negative regulatory site Ser-307. Here we demonstrate the physical association of these signaling pathways using a proteomic approach that identified insulin-regulated complexes of JIPs together with IRS scaffold proteins. Studies using mice with JIP scaffold protein defects confirm that the JIP1 and JIP2 proteins are required for normal glucose homeostasis. Together, these observations demonstrate that JIP proteins can influence insulin-stimulated signal transduction mediated by IRS proteins.

* Corresponding author. Mailing address: Howard Hughes Medical Institute, Program in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605. Phone: (508) 856-6054. Fax: (508) 856-3210. E-mail: Roger.Davis{at}umassmed.edu

{triangledown} Published ahead of print on 29 June 2009.

Molecular and Cellular Biology, September 2009, p. 4831-4840, Vol. 29, No. 17
0270-7306/09/$08.00+0     doi:10.1128/MCB.00155-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»