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Ca2+-triggered Atg11-Bmh1/2-Snf1 complex assembly initiates autophagy upon glucose starvation.
- Source :
-
The Journal of cell biology [J Cell Biol] 2024 Sep 02; Vol. 223 (9). Date of Electronic Publication: 2024 Jul 09. - Publication Year :
- 2024
-
Abstract
- Autophagy is essential for maintaining glucose homeostasis. However, the mechanism by which cells sense and respond to glucose starvation to induce autophagy remains incomplete. Here, we show that calcium serves as a fundamental triggering signal that connects environmental sensing to the formation of the autophagy initiation complex during glucose starvation. Mechanistically, glucose starvation instigates the release of vacuolar calcium into the cytoplasm, thus triggering the activation of Rck2 kinase. In turn, Rck2-mediated Atg11 phosphorylation enhances Atg11 interactions with Bmh1/2 bound to the Snf1-Sip1-Snf4 complex, leading to recruitment of vacuolar membrane-localized Snf1 to the PAS and subsequent Atg1 activation, thereby initiating autophagy. We also identified Glc7, a protein phosphatase-1, as a critical regulator of the association between Bmh1/2 and the Snf1 complex. We thus propose that calcium-triggered Atg11-Bmh1/2-Snf1 complex assembly initiates autophagy by controlling Snf1-mediated Atg1 activation in response to glucose starvation.<br /> (© 2024 Yao et al.)
- Subjects :
- Autophagy-Related Proteins metabolism
Autophagy-Related Proteins genetics
Calcium metabolism
Multiprotein Complexes metabolism
Phosphorylation
Vacuoles metabolism
Vacuoles genetics
Autophagy
Glucose metabolism
Protein Serine-Threonine Kinases metabolism
Protein Serine-Threonine Kinases genetics
Saccharomyces cerevisiae cytology
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae metabolism
Saccharomyces cerevisiae Proteins metabolism
Saccharomyces cerevisiae Proteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1540-8140
- Volume :
- 223
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- The Journal of cell biology
- Publication Type :
- Academic Journal
- Accession number :
- 38980288
- Full Text :
- https://doi.org/10.1083/jcb.202310049