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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1999-8-9
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pubmed:databankReference |
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pubmed:abstractText |
Expression cloning from a cDNA library prepared from a mutant CHO cell line with Golgi-specific resistance to Brefeldin A (BFA) identified a novel 206-kD protein with a Sec7 domain termed GBF1 for Golgi BFA resistance factor 1. Overexpression of GBF1 allowed transfected cells to maintain normal Golgi morphology and grow in the presence of BFA. Golgi- enriched membrane fractions from such transfected cells displayed normal levels of ADP ribosylation factors (ARFs) activation and coat protein recruitment that were, however, BFA resistant. Hexahistidine-tagged-GBF1 exhibited BFA-resistant guanine nucleotide exchange activity that appears specific towards ARF5 at physiological Mg2+concentration. Characterization of cDNAs recovered from the mutant and wild-type parental lines established that transcripts in these cells had identical sequence and, therefore, that GBF1 was naturally BFA resistant. GBF1 was primarily cytosolic but a significant pool colocalized to a perinuclear structure with the beta-subunit of COPI. Immunogold labeling showed highest density of GBF1 over Golgi cisternae and significant labeling over pleiomorphic smooth vesiculotubular structures. The BFA-resistant nature of GBF1 suggests involvement in retrograde traffic.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-10198630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-1409634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-1631136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-2406721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-2426273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-3042778,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-4291934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-6498939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-7440248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-7744796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-7797473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-7836400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-8027187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-8227126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-8486645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-8496147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-8576155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-8917509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-9050849,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-9268368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-9371777,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-9417041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-9425095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10402461-9539714
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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/Arf5 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Brefeldin A,
http://linkedlifedata.com/resource/pubmed/chemical/Coatomer Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sec7 guanine nucleotide exchange...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9525
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
146
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
71-84
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pubmed:dateRevised |
2010-10-8
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pubmed:meshHeading |
pubmed-meshheading:10402461-ADP-Ribosylation Factors,
pubmed-meshheading:10402461-Amino Acid Sequence,
pubmed-meshheading:10402461-Animals,
pubmed-meshheading:10402461-Biological Transport,
pubmed-meshheading:10402461-Brefeldin A,
pubmed-meshheading:10402461-CHO Cells,
pubmed-meshheading:10402461-Cell Division,
pubmed-meshheading:10402461-Cloning, Molecular,
pubmed-meshheading:10402461-Coatomer Protein,
pubmed-meshheading:10402461-Cricetinae,
pubmed-meshheading:10402461-Cytosol,
pubmed-meshheading:10402461-Drug Resistance,
pubmed-meshheading:10402461-Fungal Proteins,
pubmed-meshheading:10402461-GTP-Binding Proteins,
pubmed-meshheading:10402461-Gene Expression,
pubmed-meshheading:10402461-Golgi Apparatus,
pubmed-meshheading:10402461-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:10402461-Humans,
pubmed-meshheading:10402461-Intracellular Membranes,
pubmed-meshheading:10402461-Magnesium,
pubmed-meshheading:10402461-Male,
pubmed-meshheading:10402461-Membrane Proteins,
pubmed-meshheading:10402461-Molecular Sequence Data,
pubmed-meshheading:10402461-Proteins,
pubmed-meshheading:10402461-Rats,
pubmed-meshheading:10402461-Rats, Sprague-Dawley
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pubmed:year |
1999
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pubmed:articleTitle |
GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5.
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pubmed:affiliation |
Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7.
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