Tonks, N. K., Yang, Q., Guida, P. (1991) Structure, regulation, and function of protein tyrosine phosphatases. Cold Spring Harbor Symposia on Quantitative Biology, 56. pp. 265-273. ISSN 0091-7451
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Abstract
The phosphorylation of tyrosyl residues in proteins is an essential aspect of many signal transduction events, including the control of both normal and neoplastic cell growth and proliferation. Since the earliest observations of tyrosine phosphorylation, it has been appreciated that this is a reversible process in which the net level of phosphate in a target substrate reflects the balance between the competing action of kinases and phosphatases. Thus, in cells transformed by temperature-sensitive mutants of Rous sarcoma virus, an elevation in the levels of phosphotyrosine is observed at the permissive temperature, at which the kinase is active; however, if the cells are shifted to the nonpermissive temperature, at which the kinase is inactivated, a rapid dephosphorylation of tyrosyl residues ensues due to the action of protein tyrosine phosphatases (PTPases) (Sefton et al. 1980). The last 10 years has witnessed great progress in the characterization of the protein tyrosine kinases, whereas...
Item Type: | Paper |
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Uncontrolled Keywords: | LEUKOCYTE-COMMON ANTIGEN ROUS-SARCOMA VIRUS HUMAN-PLACENTA VIRULENCE DETERMINANT MOLECULAR-CLONING FOCAL ADHESIONS CDC25 PROTEIN T-CELLS RECEPTOR PHOSPHORYLATION |
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 > protein phosphatase 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: | 1991 |
Date Deposited: | 17 Dec 2013 15:29 |
Last Modified: | 17 Dec 2013 15:29 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/29087 |
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