<br/>Arrestin proteins are involved in multiple intracellular signaling pathways. Importantly, they have been shown to be adaptor proteins that bind phosphorylated GPCRs to inhibit G-protein coupling as well as be involved in GPCR internalization. Previous studies into arrestin-3 (Shenoy & Lefkowitz, 2005) demonstrated the importance of K11 and K12 in co-internalization of GPCRs due to being ubiquinated. However, various biochemical experiments into the double mutant K11R and K12R point to the lysines’ importance in binding and full activation. Furthermore, arrestin function and ubiquitination can be rescued by introducing mutations: R170E or E389A and D390A. To investigate the structural changes of this double mutant, I optimized the expression and purification of Arrestin-3 full-length and truncated constructs containing arginine. The purified protein will be used in X-ray crystallography studies to elucidate the structural changes incurred by introducing two arginine residues at positions 11 and 12.

Arrestin-3 co-internalization with G-protein coupled receptors is independent of Lys11 and Lys 12 ubiquitination

ACS Spring 2022

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