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

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.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Binné UK,Classon MK,Dick FA,Wei W,Rape M,Kaelin WG Jr,Näär AM,Dyson NJ

doi

10.1038/ncb1532

subject

Has Abstract

pub_date

2007-02-01 00:00:00

pages

225-32

issue

2

eissn

1465-7392

issn

1476-4679

pii

ncb1532

journal_volume

9

pub_type

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