NEDD8 modification of CUL1 dissociates p120CAND1, an inhibitor of CUL1-SKP1 binding and SCF ligases

Jidong Liu, Manabu Furukawa, Tomohiro Matsumoto, Yue Xiong

Research output: Contribution to journalArticlepeer-review

239 Scopus citations

Abstract

Cullin proteins assemble a large number of RING E3 ubiquitin ligases and regulate various physiological processes. Covalent modification of cullins by the ubiquitin-like protein NEDD8 activates cullin ligases through an as yet undefined mechanism. We show here that p120CAND1 selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation. CAND1 formed a ternary complex with CUL1 and ROC1. CAND1 dissociated SKP1 from CUL1 and inhibited SCF ligase activity in vitro. Suppression of CAND1 in vivo increased the level of the CUL1-SKP1 complex. We suggest that by restricting SKP1-CUL1 interaction, CAND1 regulated the assembly of productive SCF ubiquitin ligases, allowing a common CUL1-ROC core to be utilized by a large number of SKP1-F box-substrate subcomplexes.

Original languageEnglish (US)
Pages (from-to)1511-1518
Number of pages8
JournalMolecular Cell
Volume10
Issue number6
DOIs
StatePublished - Dec 1 2002

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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