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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 |
2001-11-14
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pubmed:abstractText |
How the occupied KDEL receptor ERD2 is sorted into COPI vesicles for Golgi-to-ER transport is largely unknown. Here, interactions between proteins of the COPI transport machinery occurring during a "wave" of transport of a KDEL ligand were studied in living cells. FRET between CFP and YFP fusion proteins was measured by multifocal multiphoton microscopy and bulk-cell spectrofluorimetry. Ligand binding induces oligomerization of ERD2 and recruitment of ARFGAP to the Golgi, where the (ERD2)n/ARFGAP complex interacts with membrane-bound ARF1. During KDEL ligand transport, interactions of ERD2 with beta-COP and p23 decrease and the proteins segregate. Both p24a and p23 interact with ARF1, but only p24 interacts with ARFGAP. These findings suggest a model for how cargo-induced oligomerization of ERD2 regulates its sorting into COPI-coated buds.
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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 Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Coat Protein Complex I,
http://linkedlifedata.com/resource/pubmed/chemical/Coatomer Protein,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/KDEL receptor,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1534-5807
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
139-53
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11703931-ADP-Ribosylation Factor 1,
pubmed-meshheading:11703931-ADP-Ribosylation Factors,
pubmed-meshheading:11703931-Animals,
pubmed-meshheading:11703931-Cercopithecus aethiops,
pubmed-meshheading:11703931-Coat Protein Complex I,
pubmed-meshheading:11703931-Coatomer Protein,
pubmed-meshheading:11703931-Cytoplasm,
pubmed-meshheading:11703931-GTPase-Activating Proteins,
pubmed-meshheading:11703931-Golgi Apparatus,
pubmed-meshheading:11703931-Ligands,
pubmed-meshheading:11703931-Membrane Proteins,
pubmed-meshheading:11703931-Peptide Fragments,
pubmed-meshheading:11703931-Protein Binding,
pubmed-meshheading:11703931-Protein Transport,
pubmed-meshheading:11703931-Receptors, Peptide,
pubmed-meshheading:11703931-Recombinant Fusion Proteins,
pubmed-meshheading:11703931-Reproducibility of Results,
pubmed-meshheading:11703931-Spectrometry, Fluorescence,
pubmed-meshheading:11703931-Vero Cells
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pubmed:year |
2001
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pubmed:articleTitle |
KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET.
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pubmed:affiliation |
Department of Neurobiology, Max-Planck-Institute of Biophysical Chemistry, Göttingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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