Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2001-1-26
pubmed:abstractText
The cytosolic coat-protein complex COP-I interacts with cytoplasmic 'retrieval' signals present in membrane proteins that cycle between the endoplasmic reticulum (ER) and the Golgi complex, and is required for both anterograde and retrograde transport in the secretory pathway. Here we study the role of COP-I in Golgi-to-ER transport of several distinct marker molecules. Microinjection of anti-COP-I antibodies inhibits retrieval of the lectin-like molecule ERGIC-53 and of the KDEL receptor from the Golgi to the ER. Transport to the ER of protein toxins, which contain a sequence that is recognized by the KDEL receptor, is also inhibited. In contrast, microinjection of anti-COP-I antibodies or expression of a GTP-restricted Arf-1 mutant does not interfere with Golgi-to-ER transport of Shiga toxin/Shiga-like toxin-1 or with the apparent recycling to the ER of Golgi-resident glycosylation enzymes. Overexpression of a GDP-restricted mutant of Rab6 blocks transport to the ER of Shiga toxin/Shiga-like toxin-1 and glycosylation enzymes, but not of ERGIC-53, the KDEL receptor or KDEL-containing toxins. These data indicate the existence of at least two distinct pathways for Golgi-to-ER transport, one COP-I dependent and the other COP-I independent. The COP-I-independent pathway is specifically regulated by Rab6 and is used by Golgi glycosylation enzymes and Shiga toxin/Shiga-like toxin-1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factor 1, http://linkedlifedata.com/resource/pubmed/chemical/Coat Protein Complex I, http://linkedlifedata.com/resource/pubmed/chemical/KDEL receptor, http://linkedlifedata.com/resource/pubmed/chemical/LMAN1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Monomeric GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals, http://linkedlifedata.com/resource/pubmed/chemical/Rab6 protein, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide, http://linkedlifedata.com/resource/pubmed/chemical/SAR1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Shiga Toxin 1, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/rab GTP-Binding Proteins
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1465-7392
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
423-30
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10559986-ADP-Ribosylation Factor 1, pubmed-meshheading:10559986-Amino Acid Motifs, pubmed-meshheading:10559986-Animals, pubmed-meshheading:10559986-Cercopithecus aethiops, pubmed-meshheading:10559986-Coat Protein Complex I, pubmed-meshheading:10559986-Endoplasmic Reticulum, pubmed-meshheading:10559986-Golgi Apparatus, pubmed-meshheading:10559986-HeLa Cells, pubmed-meshheading:10559986-Humans, pubmed-meshheading:10559986-Mannose-Binding Lectins, pubmed-meshheading:10559986-Membrane Proteins, pubmed-meshheading:10559986-Microinjections, pubmed-meshheading:10559986-Microscopy, Fluorescence, pubmed-meshheading:10559986-Monomeric GTP-Binding Proteins, pubmed-meshheading:10559986-Protein Sorting Signals, pubmed-meshheading:10559986-Protein Transport, pubmed-meshheading:10559986-Receptors, Peptide, pubmed-meshheading:10559986-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10559986-Shiga Toxin, pubmed-meshheading:10559986-Shiga Toxin 1, pubmed-meshheading:10559986-Vero Cells, pubmed-meshheading:10559986-Vesicular Transport Proteins, pubmed-meshheading:10559986-rab GTP-Binding Proteins
pubmed:year
1999
pubmed:articleTitle
Evidence for a COP-I-independent transport route from the Golgi complex to the endoplasmic reticulum.
pubmed:affiliation
Cell Biology and Biophysics Programme, EMBL Heidelberg, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't