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The ubiquitin-interacting motifs of S5a as a unique upstream inhibitor of the 26S proteasome.

Abstract：

:It has been demonstrated that ubiquitin-conjugated proteins were accumulated by ectopically-expressed S5a as well as the ubiquitin-interacting motifs of S5a (S5a-UIMs). In this study, we further found that free S5a-UIMs stabilized only a subset of proteasomal substrates including p53, c-Fos, c-Jun, and p27 but not beta-catenin, p15, and ornithine decarboxylase. Both S5a-UIMs and epoxomicin inhibited the proliferation of A549 lung cancer cells but arrest at the different stages of cell cycle. Together, our results suggest a potential role of S5a-UIMs as an upstream proteasomal inhibitor by blocking the subset of substrates from delivery to the 26S proteasome.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Elangovan M,Shin DY,Yoo YJ

doi

10.1016/j.bbrc.2009.08.078

subject

Has Abstract

pub_date

2009-10-30 00:00:00

pages

723-6

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)01646-5

journal_volume

388

pub_type

杂志文章

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