Tyrosine phosphatases and their possible interplay with tyrosine kinases

Fischer, E. H., Charbonneau, H., Cool, D. E., Tonks, N. K. (1992) Tyrosine phosphatases and their possible interplay with tyrosine kinases. Ciba Foundation Symposia, 164. pp. 132-144. ISSN 0300-5208

URL: http://www.ncbi.nlm.nih.gov/pubmed/1395930

Abstract

Protein tyrosine phosphatases represent a new family of intracellular and receptor-linked enzymes. They are totally specific toward tyrosyl residues in proteins, and, with specific activities 10-1000-fold greater than those of the protein tyrosine kinases, they can be expected to tightly control the level of phosphotyrosine within the cell. Most transmembrane forms contain two conserved intracellular catalytic domains, as displayed by the leukocyte common antigen CD45, but highly variable external segments. Some are related to the neuronal cell adhesion molecules (NCAMs) or fasciclin II and others contain fibronectin III repeats; this suggests that these enzymes might be involved in cell-cell interaction. The intracellular enzymes appear to contain a highly conserved catalytic core linked to a regulatory segment. Deletion of the regulatory domain alters both substrate specificity and cellular localization. Likewise, overexpression of the full-length and truncated enzymes affects cell cycle progression and actin filament stability, respectively. The interplay between tyrosine kinases and phosphatases is considered. A hypothesis is presented suggesting that in some systems phosphatases might act synergistically with the kinases and elicit a physiological response, irrespective of the state of phosphorylation of the target protein.

Item Type: Paper
Uncontrolled Keywords: CELL-SURFACE RECEPTORS COMMON ANTIGEN FAMILY SIGNAL TRANSDUCTION PHOSPHORYLASE-PHOSPHATASE EXTRACELLULAR-MATRIX SWISS 3T3-CELLS XENOPUS OOCYTES PROTEIN ACTIVATION COMPLEX
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > tyrosine kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: 1992
Date Deposited: 17 Dec 2013 19:37
Last Modified: 17 Dec 2013 19:37
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29082

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