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CAND1 enhances deneddylation of CUL1 by COP9 signalosome.

Abstract：

:Cullin-RING ligases (CRLs) regulate diverse cellular functions such as cell cycle progression and cytokine signaling by ubiquitinating key regulatory proteins. The activity of CRLs is controlled by Nedd8 modification of the cullin subunits. Recent reports have suggested that CAND1, which specifically binds to unmodified CUL1 but not to neddylated one, is required for the in vivo function of SCFs, the CUL1-containing CRLs. We show here that CAND1 and COP9 signalosome (CSN), the major deneddylase of cullins, bind to unneddylated CUL1 in a mutually exclusive way. The suppression of CAND1 expression by small inhibitory RNA enhanced the interaction between CUL1 and CSN, suggesting that CAND1 inhibited the binding of CSN to CUL1. We found that the binding of CSN to CUL1 required the four helix bundle in CUL1 C-terminal domain, which was wrapped around by CAND1 in the CAND1-CUL1-Rbx1 complex. CAND1 greatly facilitated CSN-mediated deneddylation of CUL1 in vitro, which was dependent on its binding to CUL1. Our data suggest that enhancement of CSN-mediated deneddylation by CAND1 may contribute to its function as a positive regulator of SCFs in vivo.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Min KW,Kwon MJ,Park HS,Park Y,Yoon SK,Yoon JB

doi

10.1016/j.bbrc.2005.06.188

subject

Has Abstract

pub_date

2005-09-02 00:00:00

pages

867-74

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01439-7

journal_volume

334

pub_type

杂志文章

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