DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAs
Summary: Glucose binding can alter protein oligomerization to enable differentiation. Here, we demonstrate that glucose binding is a general capacity of DExD/H-box RNA helicases, including DDX50, which was found to be essential for the differentiation of diverse cell types. Glucose binding to conser...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-01-01
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| Series: | Cell Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124724015250 |
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| author | Weili Miao Douglas F. Porter Zurab Siprashvili Ian D. Ferguson Luca Ducoli Duy T. Nguyen Lisa A. Ko Vanessa Lopez-Pajares Suhas Srinivasan Audrey W. Hong Yen-Yu Yang Zhongwen Cao Robin M. Meyers Jordan M. Meyers Shiying Tao Yinsheng Wang Paul A. Khavari |
| author_facet | Weili Miao Douglas F. Porter Zurab Siprashvili Ian D. Ferguson Luca Ducoli Duy T. Nguyen Lisa A. Ko Vanessa Lopez-Pajares Suhas Srinivasan Audrey W. Hong Yen-Yu Yang Zhongwen Cao Robin M. Meyers Jordan M. Meyers Shiying Tao Yinsheng Wang Paul A. Khavari |
| author_sort | Weili Miao |
| collection | DOAJ |
| description | Summary: Glucose binding can alter protein oligomerization to enable differentiation. Here, we demonstrate that glucose binding is a general capacity of DExD/H-box RNA helicases, including DDX50, which was found to be essential for the differentiation of diverse cell types. Glucose binding to conserved DDX50 ATP binding sequences altered protein conformation and dissociated DDX50 dimers. DDX50 monomers bound STAU1 to redirect STAU1 from an RNA-decay-promoting complex with UPF1 to a DDX50-STAU1 ribonuclear complex. DDX50 and STAU1 bound and stabilized a common set of essential pro-differentiation RNAs, including JUN, OVOL1, CEBPB, PRDM1, and TINCR, whose structures they also modified. These findings uncover a DDX50-mediated mechanism of reprograming STAU1 from its canonical role in Staufen-mediated mRNA decay to an opposite role stabilizing pro-differentiation RNAs and establish an activity for glucose in controlling RNA structure and stability. |
| format | Article |
| id | doaj-art-8899475619214a60802a514e9da7b2a8 |
| institution | Kabale University |
| issn | 2211-1247 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj-art-8899475619214a60802a514e9da7b2a82025-01-08T04:52:25ZengElsevierCell Reports2211-12472025-01-01441115174DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAsWeili Miao0Douglas F. Porter1Zurab Siprashvili2Ian D. Ferguson3Luca Ducoli4Duy T. Nguyen5Lisa A. Ko6Vanessa Lopez-Pajares7Suhas Srinivasan8Audrey W. Hong9Yen-Yu Yang10Zhongwen Cao11Robin M. Meyers12Jordan M. Meyers13Shiying Tao14Yinsheng Wang15Paul A. Khavari16Program in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USA; Corresponding authorProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USAProgram in Cancer Biology, Stanford University, Stanford, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USADepartment of Chemistry, University of California, Riverside, Riverside, CA, USADepartment of Chemistry, University of California, Riverside, Riverside, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USADepartment of Chemistry, University of California, Riverside, Riverside, CA, USAProgram in Epithelial Biology, Stanford University School of Medicine, Stanford, CA, USA; Program in Cancer Biology, Stanford University, Stanford, CA, USA; Veterans Affairs Palo Alto Healthcare System, Palo Alto, CA, USA; Corresponding authorSummary: Glucose binding can alter protein oligomerization to enable differentiation. Here, we demonstrate that glucose binding is a general capacity of DExD/H-box RNA helicases, including DDX50, which was found to be essential for the differentiation of diverse cell types. Glucose binding to conserved DDX50 ATP binding sequences altered protein conformation and dissociated DDX50 dimers. DDX50 monomers bound STAU1 to redirect STAU1 from an RNA-decay-promoting complex with UPF1 to a DDX50-STAU1 ribonuclear complex. DDX50 and STAU1 bound and stabilized a common set of essential pro-differentiation RNAs, including JUN, OVOL1, CEBPB, PRDM1, and TINCR, whose structures they also modified. These findings uncover a DDX50-mediated mechanism of reprograming STAU1 from its canonical role in Staufen-mediated mRNA decay to an opposite role stabilizing pro-differentiation RNAs and establish an activity for glucose in controlling RNA structure and stability.http://www.sciencedirect.com/science/article/pii/S2211124724015250CP: Molecular biology |
| spellingShingle | Weili Miao Douglas F. Porter Zurab Siprashvili Ian D. Ferguson Luca Ducoli Duy T. Nguyen Lisa A. Ko Vanessa Lopez-Pajares Suhas Srinivasan Audrey W. Hong Yen-Yu Yang Zhongwen Cao Robin M. Meyers Jordan M. Meyers Shiying Tao Yinsheng Wang Paul A. Khavari DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAs Cell Reports CP: Molecular biology |
| title | DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAs |
| title_full | DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAs |
| title_fullStr | DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAs |
| title_full_unstemmed | DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAs |
| title_short | DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAs |
| title_sort | ddx50 cooperates with stau1 to effect stabilization of pro differentiation rnas |
| topic | CP: Molecular biology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124724015250 |
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