Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing

The spindle checkpoint ensures the fidelity of chromosome segregation during mitosis and meiosis. Here the authors use a combination of biochemical and structural biology approaches to show how the TRIP13 ATPase and its adaptor, p31comet, catalyze the conversion of the checkpoint protein Mad2 betwee...

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Main Authors: Melissa L. Brulotte, Byung-Cheon Jeong, Faxiang Li, Bing Li, Eric B. Yu, Qiong Wu, Chad A. Brautigam, Hongtao Yu, Xuelian Luo
Format: Article
Language:English
Published: Nature Portfolio 2017-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02012-2
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author Melissa L. Brulotte
Byung-Cheon Jeong
Faxiang Li
Bing Li
Eric B. Yu
Qiong Wu
Chad A. Brautigam
Hongtao Yu
Xuelian Luo
author_facet Melissa L. Brulotte
Byung-Cheon Jeong
Faxiang Li
Bing Li
Eric B. Yu
Qiong Wu
Chad A. Brautigam
Hongtao Yu
Xuelian Luo
author_sort Melissa L. Brulotte
collection DOAJ
description The spindle checkpoint ensures the fidelity of chromosome segregation during mitosis and meiosis. Here the authors use a combination of biochemical and structural biology approaches to show how the TRIP13 ATPase and its adaptor, p31comet, catalyze the conversion of the checkpoint protein Mad2 between latent and active forms
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spelling doaj.art-1a45bc1b1cac4929bf939b9c726732342022-12-21T19:32:51ZengNature PortfolioNature Communications2041-17232017-12-018111410.1038/s41467-017-02012-2Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencingMelissa L. Brulotte0Byung-Cheon Jeong1Faxiang Li2Bing Li3Eric B. Yu4Qiong Wu5Chad A. Brautigam6Hongtao Yu7Xuelian Luo8Department of Pharmacology, University of Texas Southwestern Medical CenterDepartment of Pharmacology, University of Texas Southwestern Medical CenterDepartment of Pharmacology, University of Texas Southwestern Medical CenterDepartment of Pharmacology, University of Texas Southwestern Medical CenterDepartment of Pharmacology, University of Texas Southwestern Medical CenterDepartment of Biophysics, University of Texas Southwestern Medical CenterDepartment of Biophysics, University of Texas Southwestern Medical CenterDepartment of Pharmacology, University of Texas Southwestern Medical CenterDepartment of Pharmacology, University of Texas Southwestern Medical CenterThe spindle checkpoint ensures the fidelity of chromosome segregation during mitosis and meiosis. Here the authors use a combination of biochemical and structural biology approaches to show how the TRIP13 ATPase and its adaptor, p31comet, catalyze the conversion of the checkpoint protein Mad2 between latent and active formshttps://doi.org/10.1038/s41467-017-02012-2
spellingShingle Melissa L. Brulotte
Byung-Cheon Jeong
Faxiang Li
Bing Li
Eric B. Yu
Qiong Wu
Chad A. Brautigam
Hongtao Yu
Xuelian Luo
Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing
Nature Communications
title Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing
title_full Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing
title_fullStr Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing
title_full_unstemmed Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing
title_short Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing
title_sort mechanistic insight into trip13 catalyzed mad2 structural transition and spindle checkpoint silencing
url https://doi.org/10.1038/s41467-017-02012-2
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