Identification of intracellular cavin target proteins reveals cavin-PP1alpha interactions regulate apoptosis.
Caveolae is specialized domains of the plasma membrane. Invaginations formation is dependent on the expression of Caveolin-1 or -3 and protein from the family Cavin. In response to stress, caveolae dismantle and cavins released from caveolae, allowing cavins potentially interact with intracellular targets. Here, we describe the intracellular (non-plasma membrane) Purified Recombinant Protein s Cavin interactome using biotin affinity proteomics and mass spectrometry. We validate 47-interactor protein Cavin potential using cell-free expression system and the proteins that bind to the test. These data, together with analysis of pathways, revealing unknown role for the protein Cavin in metabolism and stress signals. We validated the interaction between a candidate interactor protein, protein phosphatase 1 alpha (PP1α), and Cavin-1 and -3 and showed that UV treatment causes release of caveolae Cavin3 enable interaction with and inhibition, PP1α. H2AX phosphorylation incre...