ArticleMolecular biology of the cell2019
Temporal regulation of cell polarity via the interaction of the Ras GTPase Rsr1 and the scaffold protein Bem1.
Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 38 citations in OpenAlex.
- Cdc42 interacts with chaperone Ydj1 to enhance its stability and partitioning during asymmetric cell division and aging in yeast.PLoS biology · 2026Article
- Roles for the canonical polarity machinery in the de novo establishment of polarity in budding yeast spores.Molecular biology of the cell · 2025Article
- Roles for the canonical polarity machinery in thebioRxiv : the preprint server for biology · 2025Article
- Article
- The Ras small GTPase RSR1 regulates cellulase production in Trichoderma reesei.Biotechnology for biofuels and bioproducts · 2023Article
- Gradient tracking in mating yeast depends on Bud1 inactivation and actin-independent vesicle delivery.The Journal of cell biology · 2022Article
- Up-regulation of the Cdc42 GTPase limits the replicative life span of budding yeast.Molecular biology of the cell · 2022Article
- Review
- Overexpression of theJournal of fungi (Basel, Switzerland) · 2020Article
- Article
- Regulation of Cdc42 for polarized growth in budding yeast.Microbial cell (Graz, Austria) · 2020Review
- Regulation of intrinsic polarity establishment by a differentiation-type MAPK pathway inJournal of cell science · 2020Article
- Weighted Gene Co-expression Network Analysis Identifies Critical Genes for the Production of Cellulase and Xylanase inFrontiers in microbiology · 2020Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The Cdc42 guanosine triphosphatase (GTPase) plays a central role in polarity development in species ranging from yeast to humans. In budding yeast, a specific growth site is selected in the G1 phase. Rsr1, a Ras GTPase, interacts with Cdc42 and its associated proteins to promote polarized growth at the proper bud site. Yet how Rsr1 regulates cell polarization is not fully understood. Here, we show that Rsr1-GDP interacts with the scaffold protein Bem1 in early G1, likely hindering the role of Bem1 in Cdc42 polarization and polarized secretion. Consistent with these in vivo observations, mathematical modeling predicts that Bem1 is unable to promote Cdc42 polarization in early G1 in the presence of Rsr1-GDP. We find that a part of the Bem1 Phox homology domain, which overlaps with a region interacting with the exocyst component Exo70, is necessary for the association of Bem1 with Rsr1-GDP. Overexpression of the GDP-locked Rsr1 interferes with Bem1-dependent Exo70 polarization. We thus propose that Rsr1 functions in spatial and temporal regulation of polarity establishment by associating with distinct polarity factors in its GTP- and GDP-bound states.
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