The S-nitrosylation of parkin attenuated the ubiquitination of divalent metal transporter 1 in MPP⁺-treated SH-SY5Y cells.

ABSTRACT: Abnormal iron accumulation caused by elevated levels of divalent metal transporter 1 (DMT1) contributes to progressive neurodegeneration in Parkinson's disease (PD). Parkin is a E3 ubiquitin ligase for the ubiquitination of DMT1. S-nitrosylated parkin (SNO-parkin) is commonly observed in PD. However, the effects of S-nitrosylation on the E3 ubiquitin ligase activity of parkin for the ubiquitination of DMT1 in PD are largely unknown. To elucidate the role of S-nitrosylated parkin and DMT1 in PD, SH-SY5Y cells were transfected with parkin, being treated with S-nitrosoglutathione (GSNO) and 1-methyl-4-phenylpyridinium (MPP⁺). The results showed increased levels of oxidized nitric oxide (NO) and S-nitrosylated parkin after the treatment of GSNO and MPP⁺ in parkin-transfec

SUBMITTER: Zhong Y 

PROVIDER: S-EPMC7511936 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature