Ontology highlight
ABSTRACT:
SUBMITTER: Wozniak DJ
PROVIDER: S-EPMC5688148 | biostudies-literature | 2017 Nov
REPOSITORIES: biostudies-literature
Wozniak Darren J DJ Kajdacsy-Balla Andre A Macias Virgilia V Ball-Kell Susan S Zenner Morgan L ML Bie Wenjun W Tyner Angela L AL
Nature communications 20171115 1
PTEN activity is often lost in prostate cancer. We show that the tyrosine kinase PTK6 (BRK) is a PTEN substrate. Phosphorylation of PTK6 tyrosine 342 (PY342) promotes activation, while phosphorylation of tyrosine 447 (PY447) regulates auto-inhibition. Introduction of PTEN into a PTEN null prostate cancer cell line leads to dephosphorylation of PY342 but not PY447 and PTK6 inhibition. Conversely, PTEN knockdown promotes PTK6 activation in PTEN positive cells. Using a variety of PTEN mutant constr ...[more]