Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: a novel mechanism for regulating Cdh1.

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Abstract

Exit from mitosis requires the degradation of regulatory proteins including the mitotic cyclins and securin through ubiquitination by the anaphase promoting complex (APC) bound to Cdc20 or Cdh1. Cdc20-APC is regulated through inhibition by the spindle assembly checkpoint protein MAD2. Knowledge of Cdh1-APC regulation is limited to the phosphorylation-dependent dissociation of Cdh1 from APC. We report a novel means of regulating Cdh1 by the MAD2-related gene, MAD2L2. MAD2L2 specifically binds and inhibits Cdh1-APC, paralleling the effect of MAD2 on Cdc20. We suggest that MAD2L2 and MAD2 inhibit the release of substrates from APC and propose a mechanism of inhibition.

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Journal

Journal ID (iso-abbrev): Genes Dev

Title: Genes & development

Publisher: Cold Spring Harbor Laboratory

ISSN: 0890-9369

ISSN (Print): 0890-9369

Publication date (Electronic): Jul 15 2001

Volume: 15

Issue: 14

Affiliations

[1 ] Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.

Article

DOI: 10.1101/gad.897901

PMC ID: 312740

PubMed ID: 11459825

SO-VID: 29cea61a-6f4b-493a-9747-d172f8e222a8

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