Literature DB >> 22348200

PI3K and STAT3: a new alliance.

Peter K Vogt1, Jonathan Ross Hart.   

Abstract

UNLABELLED: Recent proteomic data have uncovered an interdependence of PI3K and STAT3. In PI3K-tranformed murine cells, STAT3 is phosphorylated on Y705 and activated in a PI3K-dependent manner. Dominant negative STAT3 interferes with PI3K-induced oncogenic transformation. Phosphorylation of STAT3 in PI3K-transformed murine cells is mediated by the TEC kinase BMX. Observations on glioblastoma stem cells reveal similar critical roles for STAT3 and BMX. The new data document an important role of STAT3 in PI3K-driven oncogenic transformation and mark BMX as a promising therapeutic target that could enhance the effectiveness of PI3K inhibitors. SIGNIFICANCE: The PI3K–TOR and STAT3 signaling pathways represent two distinct regulatory networks. The discovery of a functional link between these pathways is significant for our understanding of PI3K- and STAT3-driven oncogenic mechanisms and identifies the TEC kinase BMX as a new cancer target.
© 2011 AACR.

Entities:  

Keywords:  BMX; PH domain; SILAC; TEC kinase; TOR

Mesh：

Substances：

Year:  2011        PMID： 22348200      PMCID： PMC3279943          DOI： 10.1158/2159-8290.CD-11-0218

Source DB:  PubMed          Journal:  Cancer Discov        ISSN： 2159-8274            Impact factor:   39.397


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