Abstract
PINK1, as the first reported ubiquitin kinase, can phosphorylate ubiquitin (Ub) at Ser65 site, which regulates the structure and function of Ub monomer. However, the levels of PINK1 and phosphorylated Ub (pUb) are very low in normal cells. Here we show that when proteasome activity is inhibited, the levels of soluble PINK1 (sPINK1) and pUb will increase significantly. Further we show that ubiquitin phosphorylation can inhibit the formation of K48-linked ubiquitin chains in vivo and in vitro, and the retracted state of pUb plays a leading role in the inhibition process. Ubiquitination is a necessary process for substrates degradation. Thus, phosphorylation can regulate proteasomal degradation of substrates.