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Glc7/PP1 dephosphorylates histone H3T11 to regulate autophagy and telomere silencing in response to nutrient availability.
- Source :
- Cell Discovery; 7/11/2023, Vol. 9 Issue 1, p1-25, 25p
- Publication Year :
- 2023
-
Abstract
- How cells adapt their gene expression to nutritional changes remains poorly understood. Histone H3T11 is phosphorylated by pyruvate kinase to repress gene transcription. Here, we identify the protein phosphatase 1 (PP1), Glc7 as the enzyme that specifically dephosphorylates H3T11. We also characterize two novel Glc7-containing complexes and reveal their roles in regulating gene expression upon glucose starvation. Specifically, the Glc7–Sen1 complex dephosphorylates H3T11 to activate the transcription of autophagy-related genes. The Glc7–Rif1–Rap1 complex dephosphorylates H3T11 to derepress the transcription of telomere-proximal genes. Upon glucose starvation, Glc7 expression is up-regulated and more Glc7 translocates into the nucleus to dephosphorylate H3T11, leading to induction of autophagy and derepressed transcription of telomere-proximal genes. Furthermore, the functions of PP1/Glc7 and the two Glc7-containing complexes are conserved in mammals to regulate autophagy and telomere structure. Collectively, our results reveal a novel mechanism that regulate gene expression and chromatin structure in response to glucose availability. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 20565968
- Volume :
- 9
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Cell Discovery
- Publication Type :
- Academic Journal
- Accession number :
- 164817659
- Full Text :
- https://doi.org/10.1038/s41421-023-00551-1