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Physical and functional interactions between protein tyrosine phosphatase alpha, PI 3-kinase, and PKCdelta.

Abstract：

:The somatostatin analogue, TT-232 inhibits cell proliferation and induces apoptosis in a variety of tumor cells both in vivo and in vitro. While the early transient activation of Erk/MAPK was found to be important for the induction of cell cycle arrest, the signaling pathway leading to the activation of Erk/MAPK had not been fully established. Here we present evidence that activation of the Erk/MAPK pathway by TT-232 involves PI 3-kinase, PKCdelta and the protein tyrosine phosphatase alpha (PTPalpha). We show a physical interaction of PI 3-kinase and PKCdelta with PTPalpha and show that the tyrosine phosphatase plays a role in the activation of MAPK. In this process, PTPalpha Ser-180 and Ser-204 phosphorylation is critical for the induction of phosphatase activity, which is required for dephosphorylation of pp60(c-src). Taken together, we demonstrate the physical and functional association between PI 3-kinase, PKCdelta and PTPalpha in a signaling complex that mediates the antitumor activity of the somatostatin analogue TT-232.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Steták A,Csermely P,Ullrich A,Kéri G

doi

10.1006/bbrc.2001.5811

subject

Has Abstract

pub_date

2001-11-02 00:00:00

pages

564-72

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)95811-5

journal_volume

288

pub_type

杂志文章

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