ArticleThe Journal of cell biology2021
Stress granules display bistable dynamics modulated by Cdk.
Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Cytoplasmic sequestering of a fungal stress-activated MAPK in response to a host plant phenolic acid.PLoS pathogens · 2025Article
- Rie1 and Sgn1 form an RNA-binding complex that enforces the meiotic entry cell fate decision.The Journal of cell biology · 2023Article
- Role of Ganetespib, an HSP90 Inhibitor, in Cancer Therapy: From Molecular Mechanisms to Clinical Practice.International journal of molecular sciences · 2023Review
- Review
- Heat stress reveals a specialized variant of the pachytene checkpoint in meiosis of Arabidopsis thaliana.The Plant cell · 2022Article
- Article
- eIF3a Destabilization and TDP-43 Alter Dynamics of Heat-Induced Stress Granules.International journal of molecular sciences · 2021Article
- Stress granule and P-body clearance: Seeking coherence in acts of disappearance.Seminars in cell & developmental biologyReview
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Stress granules (SGs) are conserved biomolecular condensates that originate in response to many stress conditions. These membraneless organelles contain nontranslating mRNAs and a diverse subproteome, but our knowledge of their regulation and functional relevance is still incipient. Here, we describe a mutual-inhibition interplay between SGs and Cdc28, the budding yeast Cdk. Among Cdc28 interactors acting as negative modulators of Start, we have identified Whi8, an RNA-binding protein that localizes to SGs and recruits the mRNA of CLN3, the most upstream G1 cyclin, for efficient translation inhibition and Cdk inactivation under stress. However, Whi8 also contributes to recruiting Cdc28 to SGs, where it acts to promote their dissolution. As predicted by a mutual-inhibition framework, the SG constitutes a bistable system that is modulated by Cdk. Since mammalian cells display a homologous mechanism, we propose that the opposing functions of specific mRNA-binding proteins and Cdk's subjugate SG dynamics to a conserved hysteretic switch.
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