Trotman, L. C. (2010) PTEN. In: Handbook of Cell Signaling (Second Edition). Academic Press, San Diego, pp. 849-854. ISBN 978-0-12-374145-5
Abstract
The PTEN phosphatase has an active site motif characteristic for the protein tyrosine phosphatase superfamily, yet its major substrate is the membrane lipid phosphatidylinositol (3,4,5) trisphosphate (PIP3). PTEN is thus the major antagonist of PI3 kinase signaling, which explains its supreme role in tumor suppression, development, and growth control. Research on PTEN has provided fundamental insights into many aspects of biology, such as phospholipid metabolism and the downstream signaling networks, and regulation of basic cellular processes such as migration or senescence; finally, it has even allowed the redefining of genetic principles of tumor suppression. The understanding of the PTEN pathway is expanding quickly, and has greatly profited from its high conservation in model organisms such as Dictyostelium, Caenorhabditis, and Drosophila. Mechanisms of PTEN regulation and the role of PTEN in disease recurrence after targeted therapy are now becoming clear and a conceptual framework for a successful cancer therapy is emerging. Various insights into tumor suppression strongly suggest that understanding PTEN regulation harbors great therapeutic potential, since many tumors are diagnosed while they still retain one copy of the gene. Since such efforts will require a comprehensive understanding of its biology, this chapter integrates the various facets of PTEN research.
| Item Type: | Book Section |
|---|---|
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes |
| CSHL Authors: | |
| Communities: | CSHL labs > Trotman lab |
| Depositing User: | CSHL Librarian |
| Date: | 2010 |
| Date Deposited: | 18 Oct 2011 20:56 |
| Last Modified: | 21 Feb 2017 21:48 |
| URI: | https://repository.cshl.edu/id/eprint/15543 |
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