ArticleMolecular and cellular biology1995
Isoform-specific complementation of the yeast sac6 null mutation by human fimbrin.
Article in Molecular and cellular biology, 1995. 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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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
24 citing papers in PubMed, 47 citations in OpenAlex.
- Novel Mouse Model Reveals That Serine Phosphorylation of L-Plastin Is Essential for Effective Splenic Clearance of Pneumococcus.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Genomic Study ofFrontiers in immunology · 2020Article
- LCP1 preferentially binds clasped αMβ2 integrin and attenuates leukocyte adhesion under flow.Journal of cell science · 2018Article
- Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.PLoS genetics · 2017Article
- The Structurally Plastic CH2 Domain Is Linked to Distinct Functions of Fimbrins/Plastins.The Journal of biological chemistry · 2016Article
- Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast.Nature communications · 2016Article
- Chemical proteomic identification of T-plastin as a novel host cell response factor in HCV infection.Scientific reports · 2015Article
- Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover.Molecular biology of the cell · 2014Article
- FgFim, a key protein regulating resistance to the fungicide JS399-19, asexual and sexual development, stress responses and virulence in Fusarium graminearum.Molecular plant pathology · 2014Article
- Calcium binding is essential for plastin 3 function in Smn-deficient motoneurons.Human molecular genetics · 2014Article
- Cell-cycle regulation of formin-mediated actin cable assembly.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The actin-bundling protein L-plastin supports T-cell motility and activation.Immunological reviews · 2013Review
- The actin-bundling protein L-plastin: a critical regulator of immune cell function.International journal of cell biology · 2012Article
- Prion formation and polyglutamine aggregation are controlled by two classes of genes.PLoS genetics · 2011Article
- Quantitative kinetic study of the actin-bundling protein L-plastin and of its impact on actin turn-over.PloS one · 2010Article
- Synthesis and function of membrane phosphoinositides in budding yeast, Saccharomyces cerevisiae.Biochimica et biophysica acta · 2007Review
- 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
- Expression of microbial virulence proteins in Saccharomyces cerevisiae models mammalian infection.The EMBO journal · 2001Article
- Roles of a fimbrin and an alpha-actinin-like protein in fission yeast cell polarization and cytokinesis.Molecular biology of the cell · 2001Article
- Generation of an isogenic collection of yeast actin mutants and identification of three interrelated phenotypes.Genetics · 2001Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The actin cytoskeleton is a fundamental component of eukaryotic cells, with both structural and motile roles. Actin and many of the actin-binding proteins found in different cell types are highly conserved, showing considerable similarity in both primary structure and biochemical properties. To make detailed comparisons between homologous proteins, it is necessary to know whether the various proteins are functionally, as well as structurally, conserved. Fimbrin is an example of a cytoskeletal component that, as shown by sequence determinations and biochemical characterizations, is conserved between organisms as diverse as Saccharomyces cerevisiae and humans. In this study, we examined whether the human homolog can substitute for the yeast protein in vivo. We report here that two isoforms of human fimbrin, also referred to as T- and L-plastin, can both substitute in vivo for yeast fimbrin, also known as Sac6p, whereas a third isoform, I-fimbrin (or I-plastin), cannot. We demonstrate that the human T- and L-fimbrins, in addition to complementing the temperature-sensitive growth defect of the sac6 null mutant, restore both normal cytoskeletal organization and cell shape to the mutant cells. In addition, we show that human T- and L-fimbrins can complement a sporulation defect caused by the sac6 null mutation. These findings indicate that there is a high degree of functional conservation in the cytoskeleton, even between organisms as diverse as S. cerevisiae and humans.
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