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...
Main Authors: | , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2017-12-01
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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 |
first_indexed | 2024-12-20T16:49:17Z |
format | Article |
id | doaj.art-1a45bc1b1cac4929bf939b9c72673234 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-20T16:49:17Z |
publishDate | 2017-12-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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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