ArticleMolecular and cellular biology2008
Role of nucleotide binding in septin-septin interactions and septin localization in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 51 citations in OpenAlex.
- Evolutionary degeneration of septins into pseudoGTPases: impacts on a hetero-oligomeric assembly interface.Frontiers in cell and developmental biology · 2023Article
- Reconstructed evolutionary history of the yeast septins Cdc11 and Shs1.G3 (Bethesda, Md.) · 2021Article
- Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast.eLife · 2020Article
- Registered report protocol: Quantitative analysis of septin Cdc10-associated proteome in Cryptococcus neoformans.PloS one · 2020Article
- Control of septin filament flexibility and bundling by subunit composition and nucleotide interactions.Molecular biology of the cell · 2018Article
- Septins are involved at the early stages of macroautophagy inJournal of cell science · 2018Article
- Article
- Kinetic partitioning during de novo septin filament assembly creates a critical G1 "window of opportunity" for mutant septin function.Cell cycle (Georgetown, Tex.) · 2016Article
- Detection of protein-protein interactions at the septin collar in Saccharomyces cerevisiae using a tripartite split-GFP system.Molecular biology of the cell · 2016Article
- Assembly, molecular organization, and membrane-binding properties of development-specific septins.The Journal of cell biology · 2016Article
- Comprehensive Genetic Analysis of Paralogous Terminal Septin Subunits Shs1 and Cdc11 in Saccharomyces cerevisiae.Genetics · 2015Article
- Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast.Molecular biology of the cell · 2015Article
- Off-target effects of the septin drug forchlorfenuron on nonplant eukaryotes.Eukaryotic cell · 2014Article
- Lean forward: Genetic analysis of temperature-sensitive mutants unfolds the secrets of oligomeric protein complex assembly.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014Article
- Article
- Native cysteine residues are dispensable for the structure and function of all five yeast mitotic septins.Proteins · 2013Article
- Response to "Platelets proteomics in transfusion medicine: a reality with challenging but promising future".Blood transfusion = Trasfusione del sangue · 2013Article
- Septin ring size scaling and dynamics require the coiled-coil region of Shs1p.Molecular biology of the cell · 2012Article
- Genetic interactions with mutations affecting septin assembly reveal ESCRT functions in budding yeast cytokinesis.Biological chemistry · 2011Article
- Septin structure and function in yeast and beyond.Trends in cell biology · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Septins are a conserved family of eukaryotic GTP-binding, filament-forming proteins. In Saccharomyces cerevisiae, five septins (Cdc3p, Cdc10p, Cdc11p, Cdc12p, and Shs1p) form a complex and colocalize to the incipient bud site and as a collar of filaments at the neck of budded cells. Septins serve as a scaffold to localize septin-associated proteins involved in diverse processes and as a barrier to diffusion of membrane-associated proteins. Little is known about the role of nucleotide binding in septin function. Here, we show that Cdc3p, Cdc10p, Cdc11p, and Cdc12p all bind GTP and that P-loop and G4 motif mutations affect nucleotide binding and result in temperature-sensitive defects in septin localization and function. Two-hybrid, in vitro, and in vivo analyses show that for all four septins nucleotide binding is important in septin-septin interactions and complex formation. In the absence of complete complexes, septins do not localize to the cortex, suggesting septin localization factors interact only with complete complexes. When both complete and partial complexes are present, septins localize to the cortex but do not form a collar, perhaps because of an inability to form filaments. We find no evidence that nucleotide binding is specifically involved in the interaction of septins with septin-associated proteins.
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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.