ArticleMolecular biology of the cell2012
Yeast formin Bni1p has multiple localization regions that function in polarized growth and spindle orientation.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Regulation of Cdc42 for polarized growth in budding yeast.Microbial cell (Graz, Austria) · 2020Review
- Polarisome scaffolder Spa2-mediated macromolecular condensation of Aip5 for actin polymerization.Nature communications · 2019Article
- Ratiometric GPCR signaling enables directional sensing in yeast.PLoS biology · 2019Article
- Role of Polarized G Protein Signaling in Tracking Pheromone Gradients.Developmental cell · 2015Article
- Computational model of polarized actin cables and cytokinetic actin ring formation in budding yeast.Cytoskeleton (Hoboken, N.J.) · 2015Article
- The F-BAR Cdc15 promotes contractile ring formation through the direct recruitment of the formin Cdc12.The Journal of cell biology · 2015Article
- Fertility and polarized cell growth depends on eIF5A for translation of polyproline-rich formins in Saccharomyces cerevisiae.Genetics · 2014Article
- The formins Cdc12 and For3 cooperate during contractile ring assembly in cytokinesis.The Journal of cell biology · 2013Article
- Beyond symmetry-breaking: competition and negative feedback in GTPase regulation.Trends in cell biology · 2013Review
- Article
- Myosin-V is activated by binding secretory cargo and released in coordination with Rab/exocyst function.Developmental cell · 2012Article
- Cdc42p regulation of the yeast formin Bni1p mediated by the effector Gic2p.Molecular biology of the cell · 2012Article
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3 authors at 1 institution in 1 country.
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Abstract
Formins are conserved proteins that assemble unbranched actin filaments in a regulated, localized manner. Budding yeast's two formins, Bni1p and Bnr1p, assemble actin cables necessary for polarized cell growth and organelle segregation. Here we define four regions in Bni1p that contribute to its localization to the bud and at the bud neck. The first (residues 1-333) requires dimerization for its localization and encompasses the Rho-binding domain. The second (residues 334-821) covers the Diaphanous inhibitory-dimerization-coiled coil domains, and the third is the Spa2p-binding domain. The fourth region encompasses the formin homology 1-formin homology 2-COOH region of the protein. These four regions can each localize to the bud cortex and bud neck at the right stage of the cell cycle independent of both F-actin and endogenous Bni1p. The first three regions contribute cumulatively to the proper localization of Bni1p, as revealed by the effects of progressive loss of these regions on the actin cytoskeleton and fidelity of spindle orientation. The fourth region contributes to the localization of Bni1p in tiny budded cells. Expression of mislocalized Bni1p constructs has a dominant-negative effect on both growth and nuclear segregation due to mislocalized actin assembly. These results define an unexpected complexity in the mechanism of formin localization and function.
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