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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
1998-2-2
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pubmed:databankReference |
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pubmed:abstractText |
The exocyst is a protein complex required for the late stages of secretion in yeast. Unlike the SNAREs (SNAP receptors), important secretory proteins that are broadly distributed on the target membrane, the exocyst is specifically located at sites of vesicle fusion. We have isolated cDNAs encoding the rexo70, rsec5, and rsec15 subunits of the mammalian complex. The amino acid sequences encoded by these genes are between 21% and 24% identical to their yeast homologs. All three genes are broadly expressed and multiple transcripts are observed for rexo70 and rsec15. Characterization of cDNAs encoding the 84-kDa subunit of the mammalian complex revealed a novel protein. mAbs were generated to the mammalian rsec6 subunit of the exocyst complex. rsec6 immunoreactivity is found in a punctate distribution at terminals of PC12 cell processes at or near sites of granule exocytosis.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-2047873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-3724460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-7026045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-7615633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-7748557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-7791897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-8060616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-8106408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-8221884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-8455717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-8743703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-8978675,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-8982167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-9073068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405631-9247645
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
94
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14438-43
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9405631-Amino Acid Sequence,
pubmed-meshheading:9405631-Animals,
pubmed-meshheading:9405631-Cell Membrane,
pubmed-meshheading:9405631-Cloning, Molecular,
pubmed-meshheading:9405631-DNA, Complementary,
pubmed-meshheading:9405631-Exocytosis,
pubmed-meshheading:9405631-Mammals,
pubmed-meshheading:9405631-Membrane Proteins,
pubmed-meshheading:9405631-Molecular Sequence Data,
pubmed-meshheading:9405631-Sequence Alignment,
pubmed-meshheading:9405631-Vesicular Transport Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
Subunit structure of the mammalian exocyst complex.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford CA 94305-5428, USA.
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pubmed:publicationType |
Journal Article
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