Calpain interacts with class IA phosphoinositide 3-kinases regulating their stability and signaling activity.

ABSTRACT: Class IA phosphoinositide 3-kinases (PI3Ks) are signaling enzymes with key roles in the regulation of essential cellular functions and disease, including cancer. Accordingly, their activity is tightly controlled in cells to maintain homeostasis. The formation of multiprotein complexes is a ubiquitous mechanism to regulate enzyme activity but the contribution of protein-protein interactions to the regulation of PI3K signaling is not fully understood. We designed an affinity purification quantitative mass spectrometry strategy to identify proteins interacting dynamically with PI3K in response to pathway activation, with the view that such binding partners may have a functional role in pathway regulation. Our study reveals that calpain small subunit 1 interacts with PI3K and that the associat

SUBMITTER: Beltran L 

PROVIDER: S-EPMC3182684 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature