Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85.

• DOI: 10.1128/mcb.13.12.7677
• Publication Date: 2015-10-06T00:37:17Z
• Authors: P Hu; A Mondino; E Y Skolnik; J Schlessinger
• Keywords: MAP3K7; Cyclin-dependent kinase 7; MAP2K7; Cyclin-dependent kinase 9; Cyclin-dependent kinase 4

Phosphatidylinositol 3-kinase (PI 3-kinase) has been implicated as a participant in signaling pathways regulating cell growth by virtue of its activation response to various mitogenic stimuli. Here we describe the cloning novel and ubiquitously expressed human PI 3-kinase. The 4.8-kb cDNA encodes putative translation product 1,070 amino acids which is 42% identical bovine 28% Vps34, Saccharomyces cerevisiae involved vacuolar protein sorting. Human also similar Tor2, yeast required for cycle progression. Northern (RNA) analysis demonstrated expression all tissues lines tested. Protein synthesized from an epitope-tagged had intrinsic activity associated with adaptor 85-kDa subunit (p85) intact cells, did endogenous Coprecipitation assays showed that 187-amino-acid domain between two src homology 2 domains p85 mediates interaction vitro cells. These results demonstrate existence different isoforms define family genes encoding distinct catalytic subunits can associate p85.