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Neddylation promotes protein translocation between the cytoplasm and nucleus.

Abstract：

:Neddylation is an ubiquitin-like modification of proteins that affects the activity, stability and protein-protein interaction of its substrates. Apart from its role as a promoter for Cullin ring E3 ligase to positively regulate the ubiquitylation process, other functional studies about neddylation are still lacking. In this study, we developed a system to explore the impact of neddylation on changes in the subcellular localization of proteins at the omics level. By applying a method combining subcellular protein extraction and immunoprecipitation-mass spectrometry (IP-MS), 81 proteins with a tendency to shuttle between the cytoplasm and nucleus due to different neddylation levels were obtained. Among the 81 candidates, transforming growth factor-β (TGF-β)-activated kinase 1 (TAK1) and growth arrest and DNA damage protein 45a (Gadd45a) were confirmed as novel substrates of Nedd8, and neddylation promotes TAK1 nuclear import as well as Gadd45a nuclear export.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Li S,Fang W,Cui Y,Shi H,Chen J,Li L,Zhang L,Zhang X

doi

10.1016/j.bbrc.2020.07.012

subject

Has Abstract

pub_date

2020-09-03 00:00:00

pages

991-997

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(20)31393-0

journal_volume

529

pub_type

杂志文章

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