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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2007-4-30
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pubmed:abstractText |
Herein we report that Gts1p fused with green-fluorescent protein (GFP) is localized in the cortical actin patch besides nuclei in yeast and the cortical Gts1p changed its position together with the patch depending on the cell-cycle phase, while nuclear Gts1p accumulated predominantly in the budding phase. Whereas Gts1p does not directly bind to actin, it associated mainly with the actin-associated protein Pan1p. In the GTS1-deleted transformant gts1Delta, the number of cells containing either a fragmented vacuole or an enlarged single central vacuole increased and the uptake of the hydrophilic dye Lucifer yellow (LY) in the vacuole decreased. Further, gts1Delta transformed with a mutant Gts1p having two cysteine-to-alanine substitutions in a zinc finger resembling that of GTPase-activating proteins of ADP-ribosylation factors (ARF-GAP) neither recovered the LY uptake unlike gts1Delta transformed with the wild-type GTS1, nor reduced the average size of central vacuoles as much as the latter did. These results suggested that Gts1p in the actin patch is involved in the fluid-phase endocytosis and membrane trafficking for vacuole formation and that the putative ARF-GAP domain in Gts1p plays an important role in these functions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Bicyclo Compounds, Heterocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTS1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoquinolines,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazolidines,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/latrunculin A,
http://linkedlifedata.com/resource/pubmed/chemical/lucifer yellow
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0171-9335
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
86
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
275-85
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pubmed:meshHeading |
pubmed-meshheading:17449140-ADP-Ribosylation Factors,
pubmed-meshheading:17449140-Actins,
pubmed-meshheading:17449140-Amino Acid Sequence,
pubmed-meshheading:17449140-Bicyclo Compounds, Heterocyclic,
pubmed-meshheading:17449140-Endocytosis,
pubmed-meshheading:17449140-GTPase-Activating Proteins,
pubmed-meshheading:17449140-Gene Deletion,
pubmed-meshheading:17449140-Green Fluorescent Proteins,
pubmed-meshheading:17449140-Immunoprecipitation,
pubmed-meshheading:17449140-Isoquinolines,
pubmed-meshheading:17449140-Molecular Sequence Data,
pubmed-meshheading:17449140-Protein Structure, Tertiary,
pubmed-meshheading:17449140-Protein Transport,
pubmed-meshheading:17449140-Recombinant Fusion Proteins,
pubmed-meshheading:17449140-Saccharomyces cerevisiae,
pubmed-meshheading:17449140-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:17449140-Subcellular Fractions,
pubmed-meshheading:17449140-Thiazolidines,
pubmed-meshheading:17449140-Transcription Factors,
pubmed-meshheading:17449140-Vacuoles
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pubmed:year |
2007
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pubmed:articleTitle |
Localization of Gts1p in cortical actin patches of yeast and its possible role in endocytosis.
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pubmed:affiliation |
Department of Biochemistry 2, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi 409-3898, Japan.
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pubmed:publicationType |
Journal Article
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