Dual-Specific Protein and Lipid Phosphatase PTEN and Its Biological Functions
- 1Department of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles, California 90033, USA
- 2Department of Pathology, Keck School of Medicine, University of Southern California, Los Angeles, California 90033, USA
- Correspondence: bstiles{at}usc.edu
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↵3 These authors contributed equally to this work.
Abstract
Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) encodes a 403-amino acid protein with an amino-terminal domain that shares sequence homology with the actin-binding protein tensin and the putative tyrosine-protein phosphatase auxilin. Crystal structure analysis of PTEN has revealed a C2 domain that binds to phospholipids in membranes and a phosphatase domain that displays dual-specific activity toward both tyrosine (Y), serine (S)/threonine (T), as well as lipid substrates in vitro. Characterized primarily as a lipid phosphatase, PTEN plays important roles in multiple cellular processes including cell growth/survival as well as metabolism.
