Abstract
Sjl2p is one of three yeast phosphoinositide 5'-phosphatases that belong to the conserved family of synaptojanins. Here, we show that Sjl2p is specifically associated with cortical actin patches which aggregate upon loss of the actin-regulating kinases Ark1p and Prk1p. The Sjl2p-containing clumps overlap with clathrin and early endocytic structures generated independently of NSF/Sec18p, but not with endosome- and trans Golgi network-derived membranes. Consistent with the finding that Sjl2p can bind to clathrin heavy chain in vitro, our results suggest that Sjl2p localizes to smooth endocytic vesicles that may be derived from clathrin-coated structures.
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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Adenosine Triphosphatases / metabolism
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Chromatography, Gel
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Clathrin / metabolism
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Clathrin-Coated Vesicles / metabolism
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Endocytosis / physiology*
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Endosomes / metabolism
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Fluorescent Dyes / metabolism
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Phosphoric Monoester Hydrolases / genetics
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Phosphoric Monoester Hydrolases / metabolism*
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism*
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Pyridinium Compounds / metabolism
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Quaternary Ammonium Compounds / metabolism
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Vesicular Transport Proteins / metabolism
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trans-Golgi Network / metabolism
Substances
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Actins
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Clathrin
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FM 4-64
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Fluorescent Dyes
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Pyridinium Compounds
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Quaternary Ammonium Compounds
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Vesicular Transport Proteins
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ARK1 protein, S cerevisiae
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PRK1 protein, S cerevisiae
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Protein Serine-Threonine Kinases
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INP52 protein, S cerevisiae
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Phosphoric Monoester Hydrolases
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Adenosine Triphosphatases
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SEC18 protein, S cerevisiae