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Proteasome inhibition promotes mono-ubiquitination and nuclear translocation of mature (52 kDa) PINK1.

Abstract：

:Mutations of PTEN-induced kinase 1 (PINK1) cause recessive familial Parkinson's disease. Cells lacking PINK1 display mitochondrial deficits and increased sensitivity to oxidative and proteasomal stress. It has been shown that the 52-kDa (mature) form of PINK1 in the cytoplasm mitigates proteasomal stress-induced cell death by enhancing aggresomes formation and autophagy. Here we newly demonstrate that proteasome dysfunction triggers mono-ubiquitination and nuclear translocation of mature PINK1. Enhancing PINK1 mono-ubiquitination by two different means increased nuclear accumulation of PINK1 independent of proteasome inhibition. Moreover, we show that PINK1 harbors a hitherto unknown nuclear export sequence (NES) in its C-terminus. Blocking CRM1-dependent nuclear export with leptomycin B augmented PINK1 levels in the nucleus of MG132-treated cells but not in normal cells. Overall, these results show that proteasomal stress-induced mono-ubiquitination of PINK1 mediates PINK1 nuclear translocation, while PINK1 is excluded from the nucleus of healthy cells via its NES. Therefore, mature PINK1 may have a nuclear function in cells under proteasomal stress.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sun L,Büeler H

doi

10.1016/j.bbrc.2019.07.051

subject

Has Abstract

pub_date

2019-09-17 00:00:00

pages

376-382

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(19)31401-9

journal_volume

517

pub_type

杂志文章

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