We found that PI3K Class-IA p110 alpha and p110 beta have distinct functions in myoblasts. Inhibition of p110 alpha reduced insulin-like growth factor-I (IGF-I)-stimulated Akt activity and prevented IGF-I-mediated survival in H (2)O (2)-treated cells; in contrast, siRNA knockdown of p110 beta increased IGF-I-stimulated Akt activity.

Aug 7, 2008 · Here we show that ablation of p110beta in the livers of the resulting mice leads to impaired insulin sensitivity and glucose homeostasis, while having little effect on phosphorylation of Akt, suggesting the involvement of a kinase-independent role …

Jun 25, 2008 · Here we show that ablation of p110β in the livers of the resulting mice leads to impaired insulin sensitivity and glucose homeostasis, while having little effect on phosphorylation of Akt,...

Oct 16, 2009 · We found that PI3K Class-IA p110 α and p110 β have distinct functions in myoblasts. Inhibition of p110 α reduced insulin-like growth factor-I (IGF-I)-stimulated Akt activity and prevented...

Class I PI3Ks function as heterodimers consisting of one of four catalytic p110 subunits (p110α, β, δ or γ) and a regulatory subunit [p85α (or its splice variants p55α and p50α), p85β, p55γ, p101 or p84].

Mar 4, 2011 · Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. The structure of a p110β/p85β complex identifies an inhibitory function for the C-terminal SH2 domain (cSH2) of the p85 regulatory subunit. Mutagenesis of a cSH2 contact residue activates downstream signaling in cells.

Jan 17, 2020 · In this study, we studied specific targets, the 110α and 110β subunits of PI3K, and the functions of these proteins with respect to the regulation of P-gp- and BCRP-mediated MDR during cancer treatment.

We found that PI3K Class IA p110α and p110β have distinct functions in myoblasts. Inhibition of p110α reduced IGF-I-stimulated Akt activity and prevented IGF-I-mediated survival in H 2 O 2 -treated cells; in contrast, siRNA knockdown of p110β increased IGF-I-stimulated Akt activity.

Several p110β-selective inhibitors that target the ATP binding site in the kinase domain have been identified. However, recent discoveries on the regulatory mechanisms that control p110β activity suggest alternative strategies by which to disrupt signaling by this PI 3-kinase isoform.

Using microinjection of inhibitory antibodies specific for either p110 (alpha) or p110 (beta) we have investigated the involvement of the two p110 isoforms in platelet-derived growth factor- and insulin-induced actin reorganization in porcine aortic endothelial cells.