Deubiquitinase USP54 attenuates methylmercury toxicity in human embryonic kidney 293 cells

Abstract

Deubiquitinases are an important regulator of ubiquitin-mediated signaling pathways because of their ability to cleave the isopeptide bond that connects the ubiquitin chain to the target protein. We previously reported that the expression of many proteins involved in methylmercury toxicity is regulated by the ubiquitin-proteasome system. In this study, double-stranded siRNAs against mRNAs of approximately 60 deubiquitinases were transfected into human embryonic kidney (HEK) 293 cells, and ubiquitin-specific protease 54 (USP54) was identified as a deubiquitinase that increases the sensitivity of HEK293 cells to methylmercury by RNA interference.