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rdf:type |
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lifeskim:mentions |
umls-concept:C0017837,
umls-concept:C0018296,
umls-concept:C0021400,
umls-concept:C0220843,
umls-concept:C0681814,
umls-concept:C0796516,
umls-concept:C1412323,
umls-concept:C1412536,
umls-concept:C1514562,
umls-concept:C1516048,
umls-concept:C1704675,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:dateCreated |
2006-1-17
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pubmed:abstractText |
Arl1 is a member of the Arf/Arl family of Ras-like GTPase superfamily. Arl1 is enriched in the trans-Golgi network (TGN). We have recently shown that Arl1 regulates TGN recruitment of GRIP domain-containing Golgin-97 and Golgin-245 by interacting with the conserved GRIP domain present in their carboxyl (C)-termini. We describe here methods for the analysis of the interaction between Arl1(GTP) and the GRIP domain of Golgin-245 using in vitro GST pull-down experiments. GST-Arl1(GTP) can recover endogenous Golgin-245 from HeLa cell cytosol. Furthermore, GST-GRIP domain of Golgin-245 can efficiently retain endogenous active Arl1. A pull-down assay is developed to quantify the relative level of active Arl1.
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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/ADP-ribosylation factor related...,
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Brefeldin A,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes, Immobilized,
http://linkedlifedata.com/resource/pubmed/chemical/GCC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/GOLGA4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
0076-6879
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
404
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
432-41
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pubmed:meshHeading |
pubmed-meshheading:16413289-ADP-Ribosylation Factors,
pubmed-meshheading:16413289-Animals,
pubmed-meshheading:16413289-Autoantigens,
pubmed-meshheading:16413289-Brefeldin A,
pubmed-meshheading:16413289-Cell Line,
pubmed-meshheading:16413289-Cytosol,
pubmed-meshheading:16413289-Enzymes, Immobilized,
pubmed-meshheading:16413289-Glutathione Transferase,
pubmed-meshheading:16413289-Golgi Apparatus,
pubmed-meshheading:16413289-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:16413289-HeLa Cells,
pubmed-meshheading:16413289-Humans,
pubmed-meshheading:16413289-Membrane Proteins,
pubmed-meshheading:16413289-Membrane Transport Proteins,
pubmed-meshheading:16413289-Protein Interaction Mapping,
pubmed-meshheading:16413289-Protein Structure, Tertiary,
pubmed-meshheading:16413289-Rats,
pubmed-meshheading:16413289-Recombinant Fusion Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Interaction of Arl1 GTPase with the GRIP domain of Golgin-245 as assessed by GST (glutathione-S-transferase) pull-down experiments.
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pubmed:affiliation |
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore.
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pubmed:publicationType |
Journal Article
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