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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5490
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pubmed:dateCreated |
2000-10-16
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pubmed:abstractText |
Asymmetric localization of proteins plays a key role in many cellular processes, including cell polarity and cell fate determination. Using DNA microarray analysis, we identified a plasma membrane protein-encoding mRNA (IST2) that is transported to the bud tip by an actomyosin-based process. mRNA localization created a higher concentration of IST2 protein in the bud compared with that of the mother cell, and this asymmetry was maintained by a septin-mediated membrane diffusion barrier at the mother-bud neck. These results indicate that yeast creates distinct plasma membrane compartments, as has been described in neurons and epithelial cells.
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pubmed:grant |
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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/ASH1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Actomyosin,
http://linkedlifedata.com/resource/pubmed/chemical/CDC12 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myo4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Heavy Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Type V,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
290
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
341-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11030653-Actomyosin,
pubmed-meshheading:11030653-Biological Transport,
pubmed-meshheading:11030653-Cell Compartmentation,
pubmed-meshheading:11030653-Cell Cycle,
pubmed-meshheading:11030653-Cell Cycle Proteins,
pubmed-meshheading:11030653-Cell Membrane,
pubmed-meshheading:11030653-Cytoskeletal Proteins,
pubmed-meshheading:11030653-DNA-Binding Proteins,
pubmed-meshheading:11030653-Diffusion,
pubmed-meshheading:11030653-Fungal Proteins,
pubmed-meshheading:11030653-Membrane Proteins,
pubmed-meshheading:11030653-Mutation,
pubmed-meshheading:11030653-Myosin Heavy Chains,
pubmed-meshheading:11030653-Myosin Type V,
pubmed-meshheading:11030653-Myosins,
pubmed-meshheading:11030653-Oligonucleotide Array Sequence Analysis,
pubmed-meshheading:11030653-RNA, Fungal,
pubmed-meshheading:11030653-RNA, Messenger,
pubmed-meshheading:11030653-Recombinant Fusion Proteins,
pubmed-meshheading:11030653-Repressor Proteins,
pubmed-meshheading:11030653-Saccharomyces cerevisiae,
pubmed-meshheading:11030653-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11030653-Temperature,
pubmed-meshheading:11030653-Transcription Factors
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pubmed:year |
2000
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pubmed:articleTitle |
Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier.
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pubmed:affiliation |
Department of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, CA 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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