Retinoblastoma protein and anaphase-promoting complex physically interact and functionally cooperate during cell-cycle exit - PubMed (original) (raw)

doi: 10.1038/ncb1532. Epub 2006 Dec 24.

Affiliations

PMID: 17187060
DOI: 10.1038/ncb1532

Retinoblastoma protein and anaphase-promoting complex physically interact and functionally cooperate during cell-cycle exit

Ulrich K Binné et al. Nat Cell Biol. 2007 Feb.

Erratum in

Nat Cell Biol. 2007 Mar;9(3):353

Abstract

The retinoblastoma protein (pRB) negatively regulates the progression from G1 to S phase of the cell cycle, in part, by repressing E2F-dependent transcription. pRB also possesses E2F-independent functions that contribute to cell-cycle control--for example, during pRB-mediated cell-cycle arrest pRB associates with Skp2, the F-box protein of the Skp1-Cullin-F-box protein (SCF) E3 ubiquitin ligase complex, and promotes the stability of the cyclin-dependent kinase-inhibitor p27(Kip1) through an unknown mechanism. Degradation of p27(Kip1) is mediated by ubiquitin-dependent targeting of p27(Kip1) by SCF -Skp2 (ref. 4). Here, we report a novel interaction between pRB and the anaphase-promoting complex/cyclosome (APC/C) that controls p27(Kip1) stability by targeting Skp2 for ubiquitin-mediated degradation. Cdh1, an activator of APC/C, not only interacts with pRB but is also required for a pRB-induced cell-cycle arrest. The results reveal an unexpected physical convergence between the pRB tumour-suppressor protein and E3 ligase complexes, and raise the possibility that pRB may direct APC/C to additional targets during pRB-mediated cell-cycle exit.

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Comment in

The pRb-Cdh1-p27 autoamplifying network.
Santamaría PG, Pagano M. Santamaría PG, et al. Nat Cell Biol. 2007 Feb;9(2):137-8. doi: 10.1038/ncb0207-137. Nat Cell Biol. 2007. PMID: 17268477 No abstract available.

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Retinoblastoma protein and anaphase-promoting complex physically interact and functionally cooperate during cell-cycle exit - PubMed (original) (raw)