Yeast Nuak1 phosphorylates histone H3 threonine 11 in low glucose stress by the cooperation of AMPK and CK2 signaling
Changes in available nutrients are inevitable events for most living organisms. Upon nutritional stress, several signaling pathways cooperate to change the transcription program through chromatin regulation to rewire cellular metabolism. In budding yeast, histone H3 threonine 11 phosphorylation (H3p...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2020-12-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/64588 |
| _version_ | 1811236171040161792 |
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| author | Seunghee Oh Jaehyoun Lee Selene K Swanson Laurence Florens Michael P Washburn Jerry L Workman |
| author_facet | Seunghee Oh Jaehyoun Lee Selene K Swanson Laurence Florens Michael P Washburn Jerry L Workman |
| author_sort | Seunghee Oh |
| collection | DOAJ |
| description | Changes in available nutrients are inevitable events for most living organisms. Upon nutritional stress, several signaling pathways cooperate to change the transcription program through chromatin regulation to rewire cellular metabolism. In budding yeast, histone H3 threonine 11 phosphorylation (H3pT11) acts as a marker of low glucose stress and regulates the transcription of nutritional stress-responsive genes. Understanding how this histone modification ‘senses’ external glucose changes remains elusive. Here, we show that Tda1, the yeast ortholog of human Nuak1, is a direct kinase for H3pT11 upon low glucose stress. Yeast AMP-activated protein kinase (AMPK) directly phosphorylates Tda1 to govern Tda1 activity, while CK2 regulates Tda1 nuclear localization. Collectively, AMPK and CK2 signaling converge on histone kinase Tda1 to link external low glucose stress to chromatin regulation. |
| first_indexed | 2024-04-12T12:04:22Z |
| format | Article |
| id | doaj.art-332fffdb5a464fb5a13bd15d383c97c2 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T12:04:22Z |
| publishDate | 2020-12-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-332fffdb5a464fb5a13bd15d383c97c22022-12-22T03:33:45ZengeLife Sciences Publications LtdeLife2050-084X2020-12-01910.7554/eLife.64588Yeast Nuak1 phosphorylates histone H3 threonine 11 in low glucose stress by the cooperation of AMPK and CK2 signalingSeunghee Oh0https://orcid.org/0000-0002-6701-9473Jaehyoun Lee1Selene K Swanson2Laurence Florens3Michael P Washburn4https://orcid.org/0000-0001-7568-2585Jerry L Workman5https://orcid.org/0000-0001-8163-1952Stowers Institute for Medical Research, Kansas City, United StatesStowers Institute for Medical Research, Kansas City, United StatesStowers Institute for Medical Research, Kansas City, United StatesStowers Institute for Medical Research, Kansas City, United StatesStowers Institute for Medical Research, Kansas City, United States; Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, United StatesStowers Institute for Medical Research, Kansas City, United StatesChanges in available nutrients are inevitable events for most living organisms. Upon nutritional stress, several signaling pathways cooperate to change the transcription program through chromatin regulation to rewire cellular metabolism. In budding yeast, histone H3 threonine 11 phosphorylation (H3pT11) acts as a marker of low glucose stress and regulates the transcription of nutritional stress-responsive genes. Understanding how this histone modification ‘senses’ external glucose changes remains elusive. Here, we show that Tda1, the yeast ortholog of human Nuak1, is a direct kinase for H3pT11 upon low glucose stress. Yeast AMP-activated protein kinase (AMPK) directly phosphorylates Tda1 to govern Tda1 activity, while CK2 regulates Tda1 nuclear localization. Collectively, AMPK and CK2 signaling converge on histone kinase Tda1 to link external low glucose stress to chromatin regulation.https://elifesciences.org/articles/64588histone H3 T11 phosphorylationAMPKCK2Nuak1Tda1nutrient sensing |
| spellingShingle | Seunghee Oh Jaehyoun Lee Selene K Swanson Laurence Florens Michael P Washburn Jerry L Workman Yeast Nuak1 phosphorylates histone H3 threonine 11 in low glucose stress by the cooperation of AMPK and CK2 signaling eLife histone H3 T11 phosphorylation AMPK CK2 Nuak1 Tda1 nutrient sensing |
| title | Yeast Nuak1 phosphorylates histone H3 threonine 11 in low glucose stress by the cooperation of AMPK and CK2 signaling |
| title_full | Yeast Nuak1 phosphorylates histone H3 threonine 11 in low glucose stress by the cooperation of AMPK and CK2 signaling |
| title_fullStr | Yeast Nuak1 phosphorylates histone H3 threonine 11 in low glucose stress by the cooperation of AMPK and CK2 signaling |
| title_full_unstemmed | Yeast Nuak1 phosphorylates histone H3 threonine 11 in low glucose stress by the cooperation of AMPK and CK2 signaling |
| title_short | Yeast Nuak1 phosphorylates histone H3 threonine 11 in low glucose stress by the cooperation of AMPK and CK2 signaling |
| title_sort | yeast nuak1 phosphorylates histone h3 threonine 11 in low glucose stress by the cooperation of ampk and ck2 signaling |
| topic | histone H3 T11 phosphorylation AMPK CK2 Nuak1 Tda1 nutrient sensing |
| url | https://elifesciences.org/articles/64588 |
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