ArticleMolecular biology of the cell2015
Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- Coiled-coil homo-oligomerization and disaggregase Hsp104 act in parallel to stabilize orphan septins.bioRxiv : the preprint server for biology · 2026Article
- Wild yeast isolation by middle-school students reveals features of populations residing on North American oaks.G3 (Bethesda, Md.) · 2025Article
- Stepwise order in protein complex assembly: approaches and emerging themes.Open biology · 2025Review
- Evolutionary degeneration of septins into pseudoGTPases: impacts on a hetero-oligomeric assembly interface.Frontiers in cell and developmental biology · 2023Article
- Chaperone requirements for de novo folding ofMolecular biology of the cell · 2022Article
- Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling.Molecular biology of the cell · 2021Article
- Chemical rescue of mutant proteins in living Saccharomyces cerevisiae cells by naturally occurring small molecules.G3 (Bethesda, Md.) · 2021Article
- Selective functional inhibition of a tumor-derived p53 mutant by cytosolic chaperones identified using split-YFP in budding yeast.G3 (Bethesda, Md.) · 2021Article
- Reconstructed evolutionary history of the yeast septins Cdc11 and Shs1.G3 (Bethesda, Md.) · 2021Article
- Saccharomyces spores are born prepolarized to outgrow away from spore-spore connections and penetrate the ascus wall.Yeast (Chichester, England) · 2021Article
- Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast.eLife · 2020Article
- An amphipathic helix enables septins to sense micrometer-scale membrane curvature.The Journal of cell biology · 2019Article
- A toxic imbalance of Hsp70s in Saccharomyces cerevisiae is caused by competition for cofactors.Molecular microbiology · 2017Article
- Article
- Septin complexes assemble during a kinetic window of opportunity.Cell cycle (Georgetown, Tex.) · 2016Article
- Kinetic partitioning during de novo septin filament assembly creates a critical G1 "window of opportunity" for mutant septin function.Cell cycle (Georgetown, Tex.) · 2016Article
- Coordinate action of distinct sequence elements localizes checkpoint kinase Hsl1 to the septin collar at the bud neck in Saccharomyces cerevisiae.Molecular biology of the cell · 2016Article
- Assembly, molecular organization, and membrane-binding properties of development-specific septins.The Journal of cell biology · 2016Article
- GTPase domain driven dimerization of SEPT7 is dispensable for the critical role of septins in fibroblast cytokinesis.Scientific reports · 2016Article
- Novel α-tubulin mutation disrupts neural development and tubulin proteostasis.Developmental biology · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Septin hetero-oligomers polymerize into cytoskeletal filaments with essential functions in many eukaryotic cell types. Mutations within the oligomerization interface that encompasses the GTP-binding pocket of a septin (its "G interface") cause thermoinstability of yeast septin hetero-oligomer assembly, and human disease. When coexpressed with its wild-type counterpart, a G interface mutant is excluded from septin filaments, even at moderate temperatures. We show that this quality control mechanism is specific to G interface mutants, operates during de novo septin hetero-oligomer assembly, and requires specific cytosolic chaperones. Chaperone overexpression lowers the temperature permissive for proliferation of cells expressing a G interface mutant as the sole source of a given septin. Mutations that perturb the septin G interface retard release from these chaperones, imposing a kinetic delay on the availability of nascent septin molecules for higher-order assembly. Un-expectedly, the disaggregase Hsp104 contributes to this delay in a manner that does not require its "unfoldase" activity, indicating a latent "holdase" activity toward mutant septins. These findings provide new roles for chaperone-mediated kinetic partitioning of non-native proteins and may help explain the etiology of septin-linked human diseases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.