Tonks, N. K., Yang, Q., Flint, A. J., Gebbink, M. F., Franza, B. R., Hill, D. E., Sun, H., Brady-Kalnay, S. M. (1992) Protein tyrosine phosphatases: the problems of a growing family. Cold Spring Harbor Symposia on Quantitative Biology, 57. pp. 87-94. ISSN 0091-7451
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Abstract
Protein tyrosine phosphorylation is now recognized as an important component of the control of many fundamental aspects of cellular function, including growth and differentiation, cell cycle and cytoskeletal integrity. In vivo, the net level of phosphorylation of tyrosyl residues in a target substrate reflects the balance between the competing action of kinases and phosphatases. We are examining physiological roles for protein tyrosine phosphorylation, pursuing the problem from the perspective of the enzymes that catalyze the dephosphorylation reaction, the protein tyrosine phosphatases (PTPases). The PTPases have, until recently, been somewhat neglected relative to the protein tyrosine kinases (PTKs). However, considerable progress has been made in identifying new members of the PTPase family, and it appears that they constitute a novel class of signal transducing molecules that rival the PTKs in their structural diversity and complexity. One of the principal reasons that the study of PTPases has lagged behind that of the...
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | LEUKOCYTE COMMON ANTIGEN CELL-ADHESION MOLECULE NERVOUS-SYSTEM AXONS T-CELLS E-CADHERIN ENDOPLASMIC-RETICULUM SEQUENCE-ANALYSIS MEMBRANE-PROTEIN HUMAN-PLACENTA RECEPTOR |
| 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 tyrosine phosphatase |
| CSHL Authors: | |
| Communities: | CSHL labs > Tonks lab |
| Depositing User: | Matt Covey |
| Date: | 1992 |
| Date Deposited: | 17 Dec 2013 17:56 |
| Last Modified: | 17 Dec 2013 17:56 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/29080 |
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