| First Author | Pérez-García V | Year | 2014 |
| Journal | Mol Cell Biol | Volume | 34 |
| Issue | 18 | Pages | 3359-73 |
| PubMed ID | 24958106 | Mgi Jnum | J:224357 |
| Mgi Id | MGI:5662057 | Doi | 10.1128/MCB.00167-14 |
| Citation | Perez-Garcia V, et al. (2014) Cell activation-induced phosphoinositide 3-kinase alpha/beta dimerization regulates PTEN activity. Mol Cell Biol 34(18):3359-73 |
| abstractText | The phosphoinositide 3-kinase (PI3K)/PTEN (phosphatase and tensin homolog) pathway is one of the central routes that enhances cell survival, division, and migration, and it is frequently deregulated in cancer. PI3K catalyzes formation of phosphatidylinositol 3,4,5-triphosphate [PI(3,4,5)P3] after cell activation; PTEN subsequently reduces these lipids to basal levels. Activation of the ubiquitous p110alpha isoform precedes that of p110beta at several points during the cell cycle. We studied the potential connections between p110alpha and p110beta activation, and we show that cell stimulation promotes p110alpha and p110beta association, demonstrating oligomerization of PI3K catalytic subunits within cells. Cell stimulation also promoted PTEN incorporation into this complex, which was necessary for PTEN activation. Our results show that PI3Ks dimerize in vivo and that PI3K and PTEN activities modulate each other in a complex that controls cell PI(3,4,5)P3 levels. |
