Abstract
In this study we identified a novel protein, Bsp1p, that interacts directly with two yeast synaptojanins, Sjl2p and Sjl3p, but not with Sjl1p. The interaction takes place via the Sac1/polyphosphoinositide phosphatase domain, whose conserved C-terminal region is important for binding. Subcellular localization and genetic interactions revealed a function of Bsp1p in the cortical actin cytoskeleton. A fraction of Bsp1p was found to be membrane-associated. Studies with mutants of phosphatidylinositol 4-kinase, PIK1, suggested that the interaction with membranes is facilitated by phosphoinositides. We propose that Bsp1p is an adapter that links Sjl2p and Sjl3p to the cortical actin cytoskeleton.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / metabolism*
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Adaptor Proteins, Vesicular Transport / genetics*
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Adaptor Proteins, Vesicular Transport / metabolism
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Base Sequence
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Cytoskeleton / metabolism*
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DNA Primers
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Genotype
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Kinetics
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Molecular Sequence Data
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Open Reading Frames
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Phosphatidylinositols / metabolism
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Phosphoric Monoester Hydrolases / genetics*
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Plasmids
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae Proteins / genetics*
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Saccharomyces cerevisiae Proteins / metabolism
Substances
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Actins
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Adaptor Proteins, Vesicular Transport
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Bsp1 protein, S cerevisiae
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DNA Primers
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Phosphatidylinositols
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Saccharomyces cerevisiae Proteins
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INP51 protein, S cerevisiae
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INP52 protein, S cerevisiae
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Phosphoric Monoester Hydrolases