CDC20 assists its catalytic incorporation in the mitotic checkpoint complex.


Journal

Science (New York, N.Y.)
ISSN: 1095-9203
Titre abrégé: Science
Pays: United States
ID NLM: 0404511

Informations de publication

Date de publication:
01 01 2021
Historique:
received: 07 04 2020
accepted: 18 11 2020
entrez: 1 1 2021
pubmed: 2 1 2021
medline: 12 2 2021
Statut: ppublish

Résumé

Open (O) and closed (C) topologies of HORMA-domain proteins are respectively associated with inactive and active states of fundamental cellular pathways. The HORMA protein O-MAD2 converts to C-MAD2 upon binding CDC20. This is rate limiting for assembly of the mitotic checkpoint complex (MCC), the effector of a checkpoint required for mitotic fidelity. A catalyst assembled at kinetochores accelerates MAD2:CDC20 association through a poorly understood mechanism. Using a reconstituted SAC system, we discovered that CDC20 is an impervious substrate for which access to MAD2 requires simultaneous docking on several sites of the catalytic complex. Our analysis indicates that the checkpoint catalyst is substrate assisted and promotes MCC assembly through spatially and temporally coordinated conformational changes in both MAD2 and CDC20. This may define a paradigm for other HORMA-controlled systems.

Identifiants

pubmed: 33384373
pii: 371/6524/67
doi: 10.1126/science.abc1152
doi:

Substances chimiques

BUB3 protein, human 0
Cdc20 Proteins 0
Cell Cycle Proteins 0
MAD2L1 protein, human 0
Mad2 Proteins 0
Multiprotein Complexes 0
Poly-ADP-Ribose Binding Proteins 0
CDC20 protein, human 156288-95-8
BUB1 protein, human EC 2.7.11.1
Protein Serine-Threonine Kinases EC 2.7.11.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

67-71

Informations de copyright

Copyright © 2021, American Association for the Advancement of Science.

Auteurs

Valentina Piano (V)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany. valentina.piano@mpi-dortmund.mpg.de andrea.musacchio@mpi-dortmund.mpg.de.

Amal Alex (A)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Patricia Stege (P)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Stefano Maffini (S)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Gerardo A Stoppiello (GA)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Pim J Huis In 't Veld (PJ)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Ingrid R Vetter (IR)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Andrea Musacchio (A)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany. valentina.piano@mpi-dortmund.mpg.de andrea.musacchio@mpi-dortmund.mpg.de.
Centre for Medical Biotechnology, Faculty of Biology, University Duisburg-Essen, 45141 Essen, Germany.

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Classifications MeSH