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Cytoplasmic fluidization contributes to breaking spore dormancy in fission yeast.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Jun 25; Vol. 121 (26), pp. e2405553121. Date of Electronic Publication: 2024 Jun 18. - Publication Year :
- 2024
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Abstract
- The cytoplasm is a complex, crowded environment that influences myriad cellular processes including protein folding and metabolic reactions. Recent studies have suggested that changes in the biophysical properties of the cytoplasm play a key role in cellular homeostasis and adaptation. However, it still remains unclear how cells control their cytoplasmic properties in response to environmental cues. Here, we used fission yeast spores as a model system of dormant cells to elucidate the mechanisms underlying regulation of the cytoplasmic properties. By tracking fluorescent tracer particles, we found that particle mobility decreased in spores compared to vegetative cells and rapidly increased at the onset of dormancy breaking upon glucose addition. This cytoplasmic fluidization depended on glucose-sensing via the cyclic adenosine monophosphate-protein kinase A pathway. PKA activation led to trehalose degradation through trehalase Ntp1, thereby increasing particle mobility as the amount of trehalose decreased. In contrast, the rapid cytoplasmic fluidization did not require de novo protein synthesis, cytoskeletal dynamics, or cell volume increase. Furthermore, the measurement of diffusion coefficients with tracer particles of different sizes suggests that the spore cytoplasm impedes the movement of larger protein complexes (40 to 150 nm) such as ribosomes, while allowing free diffusion of smaller molecules (~3 nm) such as second messengers and signaling proteins. Our experiments have thus uncovered a series of signaling events that enable cells to quickly fluidize the cytoplasm at the onset of dormancy breaking.<br />Competing Interests: Competing interests statement:The authors declare no competing interest.
- Subjects :
- Glucose metabolism
Cyclic AMP-Dependent Protein Kinases metabolism
Schizosaccharomyces pombe Proteins metabolism
Schizosaccharomyces pombe Proteins genetics
Signal Transduction
Spores, Fungal metabolism
Spores, Fungal physiology
Schizosaccharomyces metabolism
Schizosaccharomyces physiology
Cytoplasm metabolism
Trehalose metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1091-6490
- Volume :
- 121
- Issue :
- 26
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 38889144
- Full Text :
- https://doi.org/10.1073/pnas.2405553121