The prolyl isomerase Pin1 stabilizes NeuroD during differentiation of mechanoreceptors
The peptidyl prolyl cis-trans isomerase Pin1 plays vital roles in diverse cellular processes and pathological conditions. NeuroD is a differentiation and survival factor for a subset of neurons and pancreatic endocrine cells. Although multiple phosphorylation events are known to be crucial for Neuro...
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| Format: | Article |
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Frontiers Media S.A.
2023-09-01
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| Series: | Frontiers in Cell and Developmental Biology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fcell.2023.1225128/full |
| _version_ | 1797681910685630464 |
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| author | Liqun Zhao Steven H. Fong Steven H. Fong Qiaoyun Yang Yun-Jin Jiang Vladimir Korzh Vladimir Korzh Yih-Cherng Liou |
| author_facet | Liqun Zhao Steven H. Fong Steven H. Fong Qiaoyun Yang Yun-Jin Jiang Vladimir Korzh Vladimir Korzh Yih-Cherng Liou |
| author_sort | Liqun Zhao |
| collection | DOAJ |
| description | The peptidyl prolyl cis-trans isomerase Pin1 plays vital roles in diverse cellular processes and pathological conditions. NeuroD is a differentiation and survival factor for a subset of neurons and pancreatic endocrine cells. Although multiple phosphorylation events are known to be crucial for NeuroD function, their mechanisms remain elusive. In this study, we demonstrate that zebrafish embryos deficient in Pin1 displayed phenotypes resembling those associated with NeuroD depletion, characterized by defects in formation of mechanosensory hair cells. Furthermore, zebrafish Pin1 interacts with NeuroD in a phosphorylation-dependent manner. In Pin1-deficient cell lines, NeuroD is rapidly degraded. However, the protein stability of NeuroD is restored upon overexpression of Pin1. These findings suggest that Pin1 functionally regulates NeuroD protein levels by post-phosphorylation cis-trans isomerization during neuronal specification. |
| first_indexed | 2024-03-11T23:51:51Z |
| format | Article |
| id | doaj.art-1f9e7de275874ccaacb0fa562d39c619 |
| institution | Directory Open Access Journal |
| issn | 2296-634X |
| language | English |
| last_indexed | 2024-03-11T23:51:51Z |
| publishDate | 2023-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cell and Developmental Biology |
| spelling | doaj.art-1f9e7de275874ccaacb0fa562d39c6192023-09-19T06:08:04ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2023-09-011110.3389/fcell.2023.12251281225128The prolyl isomerase Pin1 stabilizes NeuroD during differentiation of mechanoreceptorsLiqun Zhao0Steven H. Fong1Steven H. Fong2Qiaoyun Yang3Yun-Jin Jiang4Vladimir Korzh5Vladimir Korzh6Yih-Cherng Liou7Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, SingaporeDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, SingaporeGenes and Development Division, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (A-STAR), Singapore, SingaporeDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, SingaporeInstitute of Molecular and Genomic Medicine, National Health Research Institutes, Zhunan, TaiwanDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, SingaporeGenes and Development Division, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (A-STAR), Singapore, SingaporeDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, SingaporeThe peptidyl prolyl cis-trans isomerase Pin1 plays vital roles in diverse cellular processes and pathological conditions. NeuroD is a differentiation and survival factor for a subset of neurons and pancreatic endocrine cells. Although multiple phosphorylation events are known to be crucial for NeuroD function, their mechanisms remain elusive. In this study, we demonstrate that zebrafish embryos deficient in Pin1 displayed phenotypes resembling those associated with NeuroD depletion, characterized by defects in formation of mechanosensory hair cells. Furthermore, zebrafish Pin1 interacts with NeuroD in a phosphorylation-dependent manner. In Pin1-deficient cell lines, NeuroD is rapidly degraded. However, the protein stability of NeuroD is restored upon overexpression of Pin1. These findings suggest that Pin1 functionally regulates NeuroD protein levels by post-phosphorylation cis-trans isomerization during neuronal specification.https://www.frontiersin.org/articles/10.3389/fcell.2023.1225128/fullprolyl isomerase Pin1NeuroDZebrafishcis-trans isomerizationmechanoreceptors |
| spellingShingle | Liqun Zhao Steven H. Fong Steven H. Fong Qiaoyun Yang Yun-Jin Jiang Vladimir Korzh Vladimir Korzh Yih-Cherng Liou The prolyl isomerase Pin1 stabilizes NeuroD during differentiation of mechanoreceptors Frontiers in Cell and Developmental Biology prolyl isomerase Pin1 NeuroD Zebrafish cis-trans isomerization mechanoreceptors |
| title | The prolyl isomerase Pin1 stabilizes NeuroD during differentiation of mechanoreceptors |
| title_full | The prolyl isomerase Pin1 stabilizes NeuroD during differentiation of mechanoreceptors |
| title_fullStr | The prolyl isomerase Pin1 stabilizes NeuroD during differentiation of mechanoreceptors |
| title_full_unstemmed | The prolyl isomerase Pin1 stabilizes NeuroD during differentiation of mechanoreceptors |
| title_short | The prolyl isomerase Pin1 stabilizes NeuroD during differentiation of mechanoreceptors |
| title_sort | prolyl isomerase pin1 stabilizes neurod during differentiation of mechanoreceptors |
| topic | prolyl isomerase Pin1 NeuroD Zebrafish cis-trans isomerization mechanoreceptors |
| url | https://www.frontiersin.org/articles/10.3389/fcell.2023.1225128/full |
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