Document Detail


Regulation of cell adhesion by protein-tyrosine phosphatases. I. Cell-matrix adhesion.
MedLine Citation:
PMID:  16497668     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Protein-tyrosine phosphatases are key regulators of protein tyrosine phosphorylation. More than merely terminating the pathways initiated by protein-tyrosine kinases, phosphatases are active participants in many signaling pathways. Signals involving tyrosine phosphorylation are frequently generated in response to cell-matrix adhesion. In addition, high levels of protein tyrosine phosphorylation generally promote disassembly or turnover of adhesions. In this brief review, we will discuss the role of protein-tyrosine phosphatases in cell-matrix adhesions.
Authors:
Keith Burridge; Sarita K Sastry; Jennifer L Sallee
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review     Date:  2006-02-23
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  281     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2006 Jun 
Date Detail:
Created Date:  2006-06-05     Completed Date:  2006-08-23     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15593-6     Citation Subset:  IM    
Affiliation:
Department of Cell and Developmental Biology and Lineberger Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599-7295, USA. keith_burridge@med.unc.edu
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MeSH Terms
Descriptor/Qualifier:
Cell Adhesion / physiology*
Extracellular Matrix / metabolism
Humans
Protein Tyrosine Phosphatases / metabolism,  physiology*
Signal Transduction
Grant Support
ID/Acronym/Agency:
GM29860/GM/NIGMS NIH HHS; HL45100/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
EC 3.1.3.48/Protein Tyrosine Phosphatases

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