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PPPDE1 is a novel deubiquitinase belonging to a cysteine isopeptidase family.

Abstract：

:Ubiquitinlation of proteins is prevalent and important in both normal and pathological cellular processes. Deubiquitinating enzymes (DUBs) can remove the ubiquitin tags on substrate proteins and dynamically regulate the ubiquitination process. The PPPDE family proteins were predicted to be a novel class of deubiquitinating peptidase, but this has not yet been experimentally proved. Here we validated the deubiquitinating activity of PPPDE1 and revealed its isopeptidase activity against ubiquitin conjugated through Lys 48 and Lys 63. We also identified ribosomal protein S7, RPS7, as a substrate protein of PPPDE1. Moreover, PPPDE1 could mediate the ubiquitin chain editing of RPS7, deubiquitinating Lys 48-linked ubiquitination, and finally stabilize RPS7 proteins. Taken together, we report that PPPDE1 is a novel deubiquitinase that belongs to a cysteine isopeptidase family.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Xie X,Wang X,Jiang D,Wang J,Fei R,Cong X,Wei L,Wang Y,Chen H

doi

10.1016/j.bbrc.2017.04.161

subject

Has Abstract

pub_date

2017-06-24 00:00:00

pages

291-296

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(17)30877-X

journal_volume

488

pub_type

杂志文章

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