Dual-Specific Protein and Lipid Phosphatase PTEN and Its Biological Functions
Phosphatase and tensin homolog deleted on chromosome 10 ( ) 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 d...
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Veröffentlicht in: | Cold Spring Harbor perspectives in biology 2020-01, Vol.10 (1), p.a036301 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | Phosphatase and tensin homolog deleted on chromosome 10 (
) 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. |
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ISSN: | 2157-1422 2472-5412 1943-0264 |
DOI: | 10.1101/cshperspect.a036301 |