Cited by 297Microtubule and mitosis dynamicsProtein Structure and DynamicsCancer-related Molecular Pathways

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The Mad2 spindle checkpoint protein has two distinct natively folded states

Luo, Xuelian, Tang, Zhanyun, Xia, Guohong, Wassmann, Katja, Matsumoto, Tomohiro, Rizo, Josep, Yu, Hongtao·2004·Nature Structural & Molecular Biology

DOI 10.1038/nsmb748

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Abstract

The spindle checkpoint delays chromosome segregation in response to misaligned sister chromatids during mitosis, thus ensuring the fidelity of chromosome inheritance. Through binding to Cdc20, the Mad2 spindle checkpoint protein inhibits the target of this checkpoint, the ubiquitin protein ligase APC/C(Cdc20). We now show that without cofactor binding or covalent modification Mad2 adopts two distinct folded conformations at equilibrium (termed N1-Mad2 and N2-Mad2). The structure of N2-Mad2 has been determined by NMR spectroscopy. N2-Mad2 is much more potent in APC/C inhibition. Overexpression of a Mad2 mutant that specifically sequesters N2-Mad2 partially blocks checkpoint signaling in living cells. The two Mad2 conformers interconvert slowly in vitro, but interconversion is accelerated by a fragment of Mad1, an upstream regulator of Mad2. Our results suggest that the unusual two-state behavior of Mad2 is critical for spindle checkpoint signaling.

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Self-citation

Authors: Luo, X., Tang, Z., Xia, G., Wassmann, K., Matsumoto, T., Rizo, J., & Yu, H.
Affiliations: The University of Texas Southwestern Medical Center (US)
Centre National de la Recherche Scientifique (FR)
Kyoto University (JP)
Corresponding author: Rizo, Josep
Yu, Hongtao
ORCID: Luo, Xuelian
Wassmann, Katja
Matsumoto, Tomohiro
Rizo, Josep
Yu, Hongtao
Venue: Nature Structural & Molecular Biology
Publisher: Springer Science and Business Media LLC
Published: 2004-03-14
Volume: 11
Issue: 4
Pages: 338-345
ISSN: 1545-9985 (ISSN-L)
1545-9993
DOI: 10.1038/nsmb748
OpenAlex: W2112512547
Cited by: 297
References: 42
Citations by year: 2026: 4 · 2025: 11 · 2024: 10 · 2023: 16 · 2022: 14 · 2021: 11 · 2020: 12 · 2019: 6 · 2018: 18 · 2017: 15 · 2016: 16 · 2015: 17 · 2014: 17 · 2013: 15 · 2012: 9
FWCI: 5.67
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Structural & Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Keywords: Mad2, spindle assembly checkpoint, conformational equilibrium, protein folding, CDC20, Mad1, mitosis, chromosome segregation fidelity, NMR structure
MeSH terms: Calcium-Binding Proteins, Cloning, Molecular, HeLa Cells, Humans, Spindle Apparatus, Magnetic Resonance Spectroscopy, Protein Conformation, Recombinant Proteins, Repressor Proteins, Transfection, Restriction Mapping, Cyclins, Protein Folding, Cell Cycle Proteins, Cdc20 Proteins, Mad2 Proteins

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The Mad2 spindle checkpoint protein has two distinct natively folded states

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