The deubiquitinase USP21 maintains the stemness of mouse embryonic stem cells via stabilization of Nanog
Nanog regulates embryonic stem cell (ESC) pluripotency but what controls Nanog protein stability is unclear. Here, the authors show that in mouse ESCs, Nanog protein is ubiquitinated and stabilized by the deubiquitinase USP21, which in turn is regulated by extrinsic signals, STAT3 and ERK.
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2016-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms13594 |
| _version_ | 1818952155699085312 |
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| author | Jiali Jin Jian Liu Cong Chen Zhenping Liu Cong Jiang Hongshang Chu Weijuan Pan Xinbo Wang Lingqiang Zhang Bin Li Cizhong Jiang Xin Ge Xin Xie Ping Wang |
| author_facet | Jiali Jin Jian Liu Cong Chen Zhenping Liu Cong Jiang Hongshang Chu Weijuan Pan Xinbo Wang Lingqiang Zhang Bin Li Cizhong Jiang Xin Ge Xin Xie Ping Wang |
| author_sort | Jiali Jin |
| collection | DOAJ |
| description | Nanog regulates embryonic stem cell (ESC) pluripotency but what controls Nanog protein stability is unclear. Here, the authors show that in mouse ESCs, Nanog protein is ubiquitinated and stabilized by the deubiquitinase USP21, which in turn is regulated by extrinsic signals, STAT3 and ERK. |
| first_indexed | 2024-12-20T09:45:53Z |
| format | Article |
| id | doaj.art-dc07ba8aadb9427bb2f729c5fdba7e20 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-20T09:45:53Z |
| publishDate | 2016-11-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-dc07ba8aadb9427bb2f729c5fdba7e202022-12-21T19:44:45ZengNature PortfolioNature Communications2041-17232016-11-017111510.1038/ncomms13594The deubiquitinase USP21 maintains the stemness of mouse embryonic stem cells via stabilization of NanogJiali Jin0Jian Liu1Cong Chen2Zhenping Liu3Cong Jiang4Hongshang Chu5Weijuan Pan6Xinbo Wang7Lingqiang Zhang8Bin Li9Cizhong Jiang10Xin Ge11Xin Xie12Ping Wang13Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal UniversityChinese Academy of Sciences Key Laboratory of Receptor Research, National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of SciencesShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal UniversityDepartment of Central Laboratory, Shanghai Tenth People’s Hospital of Tongji University, School of Life Science and Technology, Tongji UniversityShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal UniversityShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal UniversityShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal UniversityShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal UniversityState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Collaborative Innovation Center for Cancer MedicineKey Laboratory of Molecular Virology and Immunology, Unit of Molecular Immunology, Institute Pasteur of Shanghai, Shanghai Institutes for Biological Sciences, Chinese Academy of SciencesDepartment of Central Laboratory, Shanghai Tenth People’s Hospital of Tongji University, School of Life Science and Technology, Tongji UniversityDepartment of Clinical Medicine, Shanghai Tenth People's Hospital of Tongji University, Tongji UniversityChinese Academy of Sciences Key Laboratory of Receptor Research, National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of SciencesShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal UniversityNanog regulates embryonic stem cell (ESC) pluripotency but what controls Nanog protein stability is unclear. Here, the authors show that in mouse ESCs, Nanog protein is ubiquitinated and stabilized by the deubiquitinase USP21, which in turn is regulated by extrinsic signals, STAT3 and ERK.https://doi.org/10.1038/ncomms13594 |
| spellingShingle | Jiali Jin Jian Liu Cong Chen Zhenping Liu Cong Jiang Hongshang Chu Weijuan Pan Xinbo Wang Lingqiang Zhang Bin Li Cizhong Jiang Xin Ge Xin Xie Ping Wang The deubiquitinase USP21 maintains the stemness of mouse embryonic stem cells via stabilization of Nanog Nature Communications |
| title | The deubiquitinase USP21 maintains the stemness of mouse embryonic stem cells via stabilization of Nanog |
| title_full | The deubiquitinase USP21 maintains the stemness of mouse embryonic stem cells via stabilization of Nanog |
| title_fullStr | The deubiquitinase USP21 maintains the stemness of mouse embryonic stem cells via stabilization of Nanog |
| title_full_unstemmed | The deubiquitinase USP21 maintains the stemness of mouse embryonic stem cells via stabilization of Nanog |
| title_short | The deubiquitinase USP21 maintains the stemness of mouse embryonic stem cells via stabilization of Nanog |
| title_sort | deubiquitinase usp21 maintains the stemness of mouse embryonic stem cells via stabilization of nanog |
| url | https://doi.org/10.1038/ncomms13594 |
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