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rdf:type |
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lifeskim:mentions |
umls-concept:C0010654,
umls-concept:C0017968,
umls-concept:C0030233,
umls-concept:C0150312,
umls-concept:C1511625,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1623048,
umls-concept:C1883712
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pubmed:issue |
7
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pubmed:dateCreated |
1984-5-30
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pubmed:abstractText |
The transmembrane glycoprotein (G protein) of vesicular stomatitis virus (VSV) is known to contain 1-2 mol of covalently linked fatty acid (palmitate) per mol of protein. G protein is oriented in cellular membranes such that the carboxyl-terminal 29 amino acids protrude into the cytoplasm. We have obtained expression in eukaryotic cells of mutagenized cDNA clones that encode VSV G proteins lacking portions of this cytoplasmic domain. Labeling of these truncated proteins with [3H]palmitate indicated that the palmitate might be linked to an amino acid residue within the first 14 residues on the carboxyl-terminal side of the transmembrane domain. Using oligonucleotide directed mutagenesis, we changed the single codon specifying cysteine in this domain to a codon specifying serine. Expression of this mutant gene results in synthesis of a G protein lacking palmitate. We suggest that linkage of palmitate to G protein is through the cysteine in the cytoplasmic domain and that such a linkage may occur in many viral and cellular glycoproteins. The G protein lacking palmitate is glycosylated and is transported normally to the cell surface.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-1105573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-200844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-226266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-265521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-287008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-4204552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-4575979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6226365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6253998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6262824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6268840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6286658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6291783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6295485,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6298453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6300434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6352053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6359230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6757864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6941270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-6985476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-7023366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-7071021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6326102-7430112
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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 |
Apr
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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:volume |
81
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2050-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6326102-Amino Acid Sequence,
pubmed-meshheading:6326102-Animals,
pubmed-meshheading:6326102-DNA,
pubmed-meshheading:6326102-Fluorescent Antibody Technique,
pubmed-meshheading:6326102-Membrane Glycoproteins,
pubmed-meshheading:6326102-Mutation,
pubmed-meshheading:6326102-Palmitic Acid,
pubmed-meshheading:6326102-Palmitic Acids,
pubmed-meshheading:6326102-Transfection,
pubmed-meshheading:6326102-Vesicular stomatitis Indiana virus,
pubmed-meshheading:6326102-Viral Envelope Proteins,
pubmed-meshheading:6326102-Viral Proteins
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pubmed:year |
1984
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pubmed:articleTitle |
The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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