Phosphorylation regulates TRPV1 association with {beta}-arrestin-2

In this study, we demonstrate that phosphorylation of TRPV1 and β-arrestin-2 regulates this association at the membrane. Under serum-free media conditions, we observed a significant decrease in TRPV1 and β-arrestin-2 association in transfected CHO cells. Pharmacological activation of kinases PKA and PKC led to a robust increase in TRPV1 and β-arrestin-2 association, while inhibition of PKA and PKC decreased association. Previously, we identified potential PKA residues (S116, T370) in the N-terminus of TRPV1 modulated by β-arrestin-2. In this study we reveal that the phosphorylation status of T370 dictates β-arrestin-2 and TRPV1 association. Furthermore, we demonstrate that casein kinase 2 (CK2)-mediated phosphorylation of β-arrestin-2 at T382, is critical for its’ association with TRPV1. Taken together, our findings suggest that phosphorylation controls TRPV1 association with β-arrestin-2.

Source: BJ Cell - January 30, 2013 Category: Biochemistry Authors: E D. Por, R Gomez, A N. Akopian, N A. Jeske Tags: BJ Cell Source Type: research