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
Hauptverfasser: Tu, Taojian, Chen, Jingyu, Chen, Lulu, Stiles, Bangyan L
Format: Artikel
Sprache:eng
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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.
ISSN:2157-1422
2472-5412
1943-0264
DOI:10.1101/cshperspect.a036301