z-logo
open-access-imgOpen Access
Dual-Specific Protein and Lipid Phosphatase PTEN and Its Biological Functions
Author(s) -
Taojian Tu,
Jingyu Chen,
Lulu Chen,
Bangyan L. Stiles
Publication year - 2019
Publication title -
cold spring harbor perspectives in medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.853
H-Index - 105
eISSN - 2472-5412
pISSN - 2157-1422
DOI - 10.1101/cshperspect.a036301
Subject(s) - pten , phosphatase , dual (grammatical number) , chemistry , biochemistry , microbiology and biotechnology , biology , phosphorylation , signal transduction , art , pi3k/akt/mtor pathway , literature
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom