scholarly journals Decision letter: Histone H3 threonine 11 phosphorylation by Sch9 and CK2 regulates chronological lifespan by controlling the nutritional stress response

2018 ◽  
eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Seunghee Oh ◽  
Tamaki Suganuma ◽  
Madelaine M Gogol ◽  
Jerry L Workman

Upon nutritional stress, the metabolic status of cells is changed by nutrient signaling pathways to ensure survival. Altered metabolism by nutrient signaling pathways has been suggested to influence cellular lifespan. However, it remains unclear how chromatin regulation is involved in this process. Here, we found that histone H3 threonine 11 phosphorylation (H3pT11) functions as a marker for nutritional stress and aging. Sch9 and CK2 kinases cooperatively regulate H3pT11 under stress conditions. Importantly, H3pT11 defective mutants prolonged chronological lifespan (CLS) by altering nutritional stress responses. Thus, the phosphorylation of H3T11 by Sch9 and CK2 links a nutritional stress response to chromatin in the regulation of CLS.


2018 ◽  
Author(s):  
Seunghee Oh ◽  
Tamaki Suganuma ◽  
Madelaine M. Gogol ◽  
Jerry L. Workman

AbstractUpon nutritional stress, the metabolic status of cells is changed by nutrient signaling pathways to ensure survival. Altered metabolism by nutrient signaling pathways has been suggested to influence cellular lifespan. However, it remains unclear how chromatin regulation is involved in this process. Here, we found that histone H3 threonine 11 phosphorylation (H3pT11) functions as a marker for nutritional stress and aging. Sch9 and CK2 kinases cooperatively regulate H3pT11 under stress conditions. Importantly, H3pT11 defective mutants prolonged chronological lifespan by altering nutritional stress responses. Thus, the phosphorylation of H3T11 by Sch9 and CK2 engages a nutritional stress response to chromatin in the regulation of lifespan.


2007 ◽  
Vol 283 (6) ◽  
pp. 3454-3464 ◽  
Author(s):  
Vanina E. Alvarez ◽  
Gregor Kosec ◽  
Celso Sant'Anna ◽  
Vito Turk ◽  
Juan J. Cazzulo ◽  
...  

2008 ◽  
Vol 283 (22) ◽  
pp. 15232-15240 ◽  
Author(s):  
Sujin Lee ◽  
Myung Hee Kim ◽  
Beom Sik Kang ◽  
Jeong-Sun Kim ◽  
Ghyung-Hwa Kim ◽  
...  

2020 ◽  
Author(s):  
Seunghee Oh ◽  
Jaehyoun Lee ◽  
Selene K. Swanson ◽  
Laurence Florens ◽  
Michael P. Washburn ◽  
...  

AbstractChanges 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 orthologue of human Nuak1, is a direct kinase for H3pT11 upon low glucose stress. Yeast 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.


Sign in / Sign up

Export Citation Format

Share Document