Abstract
In this report, we have shown that the yeast amphiphysin-like protein Rvs167p was localized mainly in small cortical patches throughout the cell in unbudding cells. During budding, the patches were polarized at bud emergence site. During mating, Rvs167p was concentrated at the tip of the shmoo. Rvs167p colocalized with actin patches during yeast vegetative growth and mating. Complete disruption of the actin cytoskeleton using Latrunculin-A did not affect Rvs167p localization in patches throughout the cell. In rvs167 mutant cells, actin patches are mislocalized and in rvs161 or abp1 mutant cells, Rvs167p localization is not affected. These observations suggest that Rvs167p may localize the actin cortical complex properly. Finally, the amphiphysin-conserved N-terminal domain of Rvs167p, called the BAR domain, was required but not sufficient for the correct localization of the protein.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / analysis
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Actins / physiology*
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Bridged Bicyclo Compounds, Heterocyclic / pharmacology
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Cell Division
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Cytoskeleton / drug effects
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Cytoskeleton / ultrastructure
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Fungal Proteins / analysis
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Fungal Proteins / genetics
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Fungal Proteins / physiology*
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Genotype
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Green Fluorescent Proteins
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Luminescent Proteins / analysis
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Marine Toxins / pharmacology
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Microfilament Proteins
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Nerve Tissue Proteins / physiology
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Polymerase Chain Reaction
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Recombinant Fusion Proteins / analysis
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / physiology*
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Saccharomyces cerevisiae / ultrastructure*
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Saccharomyces cerevisiae Proteins*
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Thiazoles / pharmacology
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Thiazolidines
Substances
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Actins
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Bridged Bicyclo Compounds, Heterocyclic
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Fungal Proteins
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Luminescent Proteins
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Marine Toxins
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Microfilament Proteins
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Nerve Tissue Proteins
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RVS167 protein, S cerevisiae
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Thiazoles
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Thiazolidines
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Green Fluorescent Proteins
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amphiphysin
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latrunculin A