The structural flexibility of MAD1 facilitates the assembly of the Mitotic Checkpoint Complex.


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
18 03 2023
Historique:
received: 26 06 2022
accepted: 08 03 2023
entrez: 19 3 2023
pubmed: 20 3 2023
medline: 22 3 2023
Statut: epublish

Résumé

The spindle assembly checkpoint (SAC) safeguards the genome during cell division by generating an effector molecule known as the Mitotic Checkpoint Complex (MCC). The MCC comprises two subcomplexes: BUBR1:BUB3 and CDC20:MAD2, and the formation of CDC20:MAD2 is the rate-limiting step during MCC assembly. Recent studies show that the rate of CDC20:MAD2 formation is significantly accelerated by the cooperative binding of CDC20 to the SAC proteins MAD1 and BUB1. However, the molecular basis for this acceleration is not fully understood. Here, we demonstrate that the structural flexibility of MAD1 at a conserved hinge near the C-terminus is essential for catalytic MCC assembly. This MAD1 hinge enables the MAD1:MAD2 complex to assume a folded conformation in vivo. Importantly, truncating the hinge reduces the rate of MCC assembly in vitro and SAC signaling in vivo. Conversely, mutations that preserve hinge flexibility retain SAC signaling, indicating that the structural flexibility of the hinge, rather than a specific amino acid sequence, is important for SAC signaling. We summarize these observations as the 'knitting model' that explains how the folded conformation of MAD1:MAD2 promotes CDC20:MAD2 assembly.

Identifiants

pubmed: 36934097
doi: 10.1038/s41467-023-37235-z
pii: 10.1038/s41467-023-37235-z
pmc: PMC10024682
doi:

Substances chimiques

Protein Serine-Threonine Kinases EC 2.7.11.1
Cell Cycle Proteins 0
Mad2 Proteins 0
Cdc20 Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

1529

Subventions

Organisme : U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS)
ID : R35-GM-126983

Informations de copyright

© 2023. The Author(s).

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Auteurs

Chu Chen (C)

Biophysics, University of Michigan, Ann Arbor, MI, 48109, USA.
Department of Molecular Genetics of Ageing, Max Planck Institute for Biology of Ageing, Cologne, 50931, Germany.

Valentina Piano (V)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
Institute of Human Genetics, University Hospital Cologne, Cologne, 50931, Germany.

Amal Alex (A)

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

Simon J Y Han (SJY)

Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA.
Medical Scientist Training Program, University of Cincinnati College of Medicine, Cincinnati, OH, 45267, USA.

Pim J Huis In 't Veld (PJ)

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

Babhrubahan Roy (B)

Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA.

Daniel Fergle (D)

Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA.

Andrea Musacchio (A)

Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
Centre for Medical Biotechnology, Faculty of Biology, University Duisburg-Essen, Essen, 45141, Germany.

Ajit P Joglekar (AP)

Biophysics, University of Michigan, Ann Arbor, MI, 48109, USA. ajitj@umich.edu.
Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA. ajitj@umich.edu.

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