A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP II
The SMN protein recognizes symmetric dimethylarginine by its Tudor domain, and SMN deficiency leads to spinal muscular atrophy. Here, Liu et al. discover a small molecule that binds to the SMN Tudor domain and disrupts the interaction between SMN and RNA Polymerase II.
Main Authors: | , , , , , , , , , , , , , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2022-09-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-022-33229-5 |
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author | Yanli Liu Aman Iqbal Weiguo Li Zuyao Ni Yalong Wang Jurupula Ramprasad Karan Joshua Abraham Mengmeng Zhang Dorothy Yanling Zhao Su Qin Peter Loppnau Honglv Jiang Xinghua Guo Peter J. Brown Xuechu Zhen Guoqiang Xu Karim Mekhail Xingyue Ji Mark T. Bedford Jack F. Greenblatt Jinrong Min |
author_facet | Yanli Liu Aman Iqbal Weiguo Li Zuyao Ni Yalong Wang Jurupula Ramprasad Karan Joshua Abraham Mengmeng Zhang Dorothy Yanling Zhao Su Qin Peter Loppnau Honglv Jiang Xinghua Guo Peter J. Brown Xuechu Zhen Guoqiang Xu Karim Mekhail Xingyue Ji Mark T. Bedford Jack F. Greenblatt Jinrong Min |
author_sort | Yanli Liu |
collection | DOAJ |
description | The SMN protein recognizes symmetric dimethylarginine by its Tudor domain, and SMN deficiency leads to spinal muscular atrophy. Here, Liu et al. discover a small molecule that binds to the SMN Tudor domain and disrupts the interaction between SMN and RNA Polymerase II. |
first_indexed | 2024-04-12T21:04:02Z |
format | Article |
id | doaj.art-a0e6fffeffbb41e8b6c0ef99920dda4b |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-04-12T21:04:02Z |
publishDate | 2022-09-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-a0e6fffeffbb41e8b6c0ef99920dda4b2022-12-22T03:16:45ZengNature PortfolioNature Communications2041-17232022-09-0113111210.1038/s41467-022-33229-5A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP IIYanli Liu0Aman Iqbal1Weiguo Li2Zuyao Ni3Yalong Wang4Jurupula Ramprasad5Karan Joshua Abraham6Mengmeng Zhang7Dorothy Yanling Zhao8Su Qin9Peter Loppnau10Honglv Jiang11Xinghua Guo12Peter J. Brown13Xuechu Zhen14Guoqiang Xu15Karim Mekhail16Xingyue Ji17Mark T. Bedford18Jack F. Greenblatt19Jinrong Min20Jiangsu Key Laboratory of Neuropsychiatric Diseases and College of Pharmaceutical Sciences, Soochow UniversityStructural Genomics Consortium, University of TorontoHubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal UniversityDonnelly Centre, University of TorontoDepartment of Epigenetics and Molecular Carcinogenesis, The University of Texas MD Anderson Cancer CenterJiangsu Key Laboratory of Neuropsychiatric Diseases and College of Pharmaceutical Sciences, Soochow UniversityDepartment of Laboratory Medicine and Pathobiology, Faculty of Medicine, University of TorontoJiangsu Key Laboratory of Neuropsychiatric Diseases and College of Pharmaceutical Sciences, Soochow UniversityDonnelly Centre, University of TorontoStructural Genomics Consortium, University of TorontoStructural Genomics Consortium, University of TorontoJiangsu Key Laboratory of Neuropsychiatric Diseases and College of Pharmaceutical Sciences, Soochow UniversityDonnelly Centre, University of TorontoStructural Genomics Consortium, University of TorontoJiangsu Key Laboratory of Neuropsychiatric Diseases and College of Pharmaceutical Sciences, Soochow UniversityJiangsu Key Laboratory of Neuropsychiatric Diseases and College of Pharmaceutical Sciences, Soochow UniversityDepartment of Laboratory Medicine and Pathobiology, Faculty of Medicine, University of TorontoJiangsu Key Laboratory of Neuropsychiatric Diseases and College of Pharmaceutical Sciences, Soochow UniversityDepartment of Epigenetics and Molecular Carcinogenesis, The University of Texas MD Anderson Cancer CenterDonnelly Centre, University of TorontoHubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal UniversityThe SMN protein recognizes symmetric dimethylarginine by its Tudor domain, and SMN deficiency leads to spinal muscular atrophy. Here, Liu et al. discover a small molecule that binds to the SMN Tudor domain and disrupts the interaction between SMN and RNA Polymerase II.https://doi.org/10.1038/s41467-022-33229-5 |
spellingShingle | Yanli Liu Aman Iqbal Weiguo Li Zuyao Ni Yalong Wang Jurupula Ramprasad Karan Joshua Abraham Mengmeng Zhang Dorothy Yanling Zhao Su Qin Peter Loppnau Honglv Jiang Xinghua Guo Peter J. Brown Xuechu Zhen Guoqiang Xu Karim Mekhail Xingyue Ji Mark T. Bedford Jack F. Greenblatt Jinrong Min A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP II Nature Communications |
title | A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP II |
title_full | A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP II |
title_fullStr | A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP II |
title_full_unstemmed | A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP II |
title_short | A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP II |
title_sort | small molecule antagonist of smn disrupts the interaction between smn and rnap ii |
url | https://doi.org/10.1038/s41467-022-33229-5 |
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