ISI Web of Knowledge Take the next step  
Web of Science®
 
Previous Record (inactive) Record 1  of  1 Next Record (inactive)
Record from Web of Science®
Suppression of integrin activation: A novel function of a Ras/Raf-initiated MAP kinase pathway
Author(s): Hughes PE, Renshaw MW, Pfaff M, Forsyth J, Keivens VM, Schwartz MA, Ginsberg MH
Source: CELL    Volume: 88    Issue: 4    Pages: 521-530    Published: FEB 21 1997  
Times Cited: 349     References: 46     
Abstract: Rapid modulation of ligand binding affinity (''activation'') is a central property of the integrin cell adhesion receptors. Using a screen for suppressors of integrin activation, we identified the small GTP-binding protein, H-Ras, and its effector kinase, Raf-l, as negative regulators of integrin activation. H-Ras inhibited the activation of integrins with three distinct alpha and beta subunit cytoplasmic domains. Suppression was not associated with integrin phosphorylation and was independent of both mRNA transcription and protein synthesis. Furthermore, suppression correlated with activation of the ERK MAP kinase pathway. Thus, regulation of integrin affinity state is a novel, transcription-independent function of a Ras-linked MAP kinase pathway that may mediate a negative feedback loop in integrin function.
Document Type: Article
Language: English
Addresses:
1. Scripps Res Inst, DEPT VASC BIOL, LA JOLLA, CA 92037 USA
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: WJ691
ISSN: 0092-8674
Previous Record (inactive) Record 1  of  1 Next Record (inactive)
Record from Web of Science®
  
Thomson Reuters Logo