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J. Biol. Chem., Vol. 281, Issue 23, 15593-15596, June 9, 2006

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Minireview

Regulation of Cell Adhesion by Protein-tyrosine Phosphatases

I. CELL-MATRIX ADHESION^*

Keith Burridge¹, Sarita K. Sastry, and Jennifer L. Sallee²

From the Department of Cell and Developmental Biology and Lineberger Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599-7295 and the Department of Biochemistry and Molecular Biology and University of Texas Medical Branch Sealy Center for Cancer Cell Biology, University of Texas, Galveston, Texas 77555-1048

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.

^* This minireview will be reprinted in the 2006 Minireview Compendium, which will be available in January, 2007. This work was supported in part by National Institutes of Health Grants GM29860 and HL45100. This is Paper I in the series "Regulation of Cell Adhesion by Protein-tyrosine Phosphatases." Ref. 3 is Paper II in this series.

² Holds a predoctoral fellowship from the American Heart Association.

¹ To whom correspondence should be addressed: Dept. of Cell and Developmental Biology, University of North Carolina, Chapel Hill, NC 27599-7295. Tel.: 919-966-5783; E-mail: keith_burridge{at}med.unc.edu.

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