ArticleMolecular biology of the cell1993
Unexpected combinations of null mutations in genes encoding the actin cytoskeleton are lethal in yeast.
Article in Molecular biology of the cell, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 54 citations in OpenAlex.
- Dynamic remodeling of actin networks by cyclase-associated protein and CAP-Abp1 complexes.Current biology : CB · 2023Article
- Genetically inspired in vitro reconstitution ofMolecular biology of the cell · 2020Article
- Yeast genetic interaction screens in the age of CRISPR/Cas.Current genetics · 2019Review
- The actin capping protein in Aspergillus nidulans enhances dynein function without significantly affecting Arp1 filament assembly.Scientific reports · 2018Article
- Role of actin-bundling protein Sac6 in growth of Cryptococcus neoformans at low oxygen concentration.Eukaryotic cell · 2012Article
- Vital role for the Plasmodium actin capping protein (CP) beta-subunit in motility of malaria sporozoites.Molecular microbiology · 2009Article
- Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments.Molecular biology of the cell · 2006Article
- Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions.Molecular biology of the cell · 2005Article
- Capping protein binding to actin in yeast: biochemical mechanism and physiological relevance.The Journal of cell biology · 2004Article
- The Rho-GAP Bem2p plays a GAP-independent role in the morphogenesis checkpoint.The EMBO journal · 2002Article
- Interactions among a fimbrin, a capping protein, and an actin-depolymerizing factor in organization of the fission yeast actin cytoskeleton.Molecular biology of the cell · 2001Article
- Roles of a fimbrin and an alpha-actinin-like protein in fission yeast cell polarization and cytokinesis.Molecular biology of the cell · 2001Article
- Aip1p interacts with cofilin to disassemble actin filaments.The Journal of cell biology · 1999Article
- Assembly and function of the actin cytoskeleton of yeast: relationships between cables and patches.The Journal of cell biology · 1998Article
- Depolarization of the actin cytoskeleton is a specific phenotype in Saccharomyces cerevisiae.Journal of cell science · 1998Article
- Mutations synthetically lethal with tpm1delta lie in genes involved in morphogenesis.Genetics · 1997Article
- The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton.The Journal of cell biology · 1997Article
- The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton.The Journal of cell biology · 1996Article
- BRO1, a novel gene that interacts with components of the Pkc1p-mitogen-activated protein kinase pathway in Saccharomyces cerevisiae.Molecular and cellular biology · 1996Article
- Movement of cortical actin patches in yeast.The Journal of cell biology · 1996Article
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3 authors at 1 institution in 1 country.
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Abstract
To understand the role of the actin cytoskeleton in cell physiology, and how actin-binding proteins regulate the actin cytoskeleton in vivo, we and others previously identified actin-binding proteins in Saccharomyces cerevisiae and studied the effect of null mutations in the genes for these proteins. A null mutation of the actin gene (ACT1) is lethal, but null mutations in the tropomyosin (TPM1), fimbrin (SAC6), Abp1p (ABP1), and capping protein (CAP1 and CAP2) genes have relatively mild or no effects. We have now constructed double and triple mutants lacking 2 or 3 of these actin-binding proteins, and studied the effect of the combined mutations on cell growth, morphology, and organization of the actin cytoskeleton. Double mutants lacking fimbrin and either Abp1p or capping protein show negative synthetic effects on growth, in the most extreme case resulting in lethality. All other combinations of double mutations and the triple mutant lacking tropomyosin, Abp1p, and capping protein, are viable and their phenotypes are similar to or only slightly more severe than those of the single mutants. Therefore, the synthetic phenotypes are highly specific. We confirmed this specificity by overexpression of capping protein and Abp1p in strains lacking fimbrin. Thus, while overexpression of these proteins has deleterious effects on actin organization in wild-type strains, no synthetic phenotype was observed in the absence of fimbrin. We draw two important conclusions from these results. First, since mutations in pairs of actin-binding protein genes cause inviability, the actin cytoskeleton of yeast does not contain a high degree of redundancy. Second, the lack of structural and functional homology among these genetically redundant proteins (fimbrin and capping protein or Abp1p) indicates that they regulate the actin cytoskeleton by different mechanisms. Determination of the molecular basis for this surprising conclusion will provide unique insights into the essential mechanisms that regulate the actin cytoskeleton.
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