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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
48
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pubmed:dateCreated |
2005-11-28
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pubmed:databankReference |
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pubmed:abstractText |
Through a proteomic analysis of clathrin-coated vesicles from rat liver we identified the mammalian homolog of receptor-mediated endocytosis 8 (RME-8), a DnaJ domain-containing protein originally identified in a screen for endocytic defects in Caenorhabditis elegans. Mammalian RME-8 has a broad tissue distribution, and affinity selection assays reveal the ubiquitous chaperone Hsc70, which regulates protein conformation at diverse membrane sites as the major binding partner for its DnaJ domain. RME-8 is tightly associated with microsomal membranes and co-localizes with markers of the endosomal system. Small interfering RNA-mediated knock down of RME-8 has no influence on transferrin endocytosis but causes a reduction in epidermal growth factor internalization. Interestingly, and consistent with a localization to endosomes, knock down of RME-8 also leads to alterations in the trafficking of the cation-independent mannose 6-phosphate receptor and improper sorting of the lysosomal hydrolase cathepsin D. Our data demonstrate that RME-8 functions in intracellular trafficking and provides the first evidence of a functional role for a DnaJ domain-bearing co-chaperone on endosomes.
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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/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin D,
http://linkedlifedata.com/resource/pubmed/chemical/Cations,
http://linkedlifedata.com/resource/pubmed/chemical/Cholera Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/HSC70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP40 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/RME-8 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
40135-43
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:16179350-Amino Acid Sequence,
pubmed-meshheading:16179350-Animals,
pubmed-meshheading:16179350-Biological Transport,
pubmed-meshheading:16179350-COS Cells,
pubmed-meshheading:16179350-Caenorhabditis elegans,
pubmed-meshheading:16179350-Caenorhabditis elegans Proteins,
pubmed-meshheading:16179350-Cathepsin D,
pubmed-meshheading:16179350-Cations,
pubmed-meshheading:16179350-Cell Membrane,
pubmed-meshheading:16179350-Cell Separation,
pubmed-meshheading:16179350-Cercopithecus aethiops,
pubmed-meshheading:16179350-Cholera Toxin,
pubmed-meshheading:16179350-Clathrin,
pubmed-meshheading:16179350-DNA, Complementary,
pubmed-meshheading:16179350-Endocytosis,
pubmed-meshheading:16179350-Endosomes,
pubmed-meshheading:16179350-Epidermal Growth Factor,
pubmed-meshheading:16179350-Flow Cytometry,
pubmed-meshheading:16179350-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:16179350-Fluorescent Dyes,
pubmed-meshheading:16179350-Glutathione Transferase,
pubmed-meshheading:16179350-HSC70 Heat-Shock Proteins,
pubmed-meshheading:16179350-HSP40 Heat-Shock Proteins,
pubmed-meshheading:16179350-Humans,
pubmed-meshheading:16179350-Liver,
pubmed-meshheading:16179350-Lysosomes,
pubmed-meshheading:16179350-Microscopy, Fluorescence,
pubmed-meshheading:16179350-Microsomes, Liver,
pubmed-meshheading:16179350-Molecular Chaperones,
pubmed-meshheading:16179350-Molecular Sequence Data,
pubmed-meshheading:16179350-Protein Binding,
pubmed-meshheading:16179350-Protein Conformation,
pubmed-meshheading:16179350-Protein Structure, Tertiary,
pubmed-meshheading:16179350-Proteomics,
pubmed-meshheading:16179350-RNA, Small Interfering,
pubmed-meshheading:16179350-Rats,
pubmed-meshheading:16179350-Receptor, IGF Type 2,
pubmed-meshheading:16179350-Recombinant Fusion Proteins,
pubmed-meshheading:16179350-Subcellular Fractions,
pubmed-meshheading:16179350-Tissue Distribution,
pubmed-meshheading:16179350-Transferrin
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pubmed:year |
2005
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pubmed:articleTitle |
The DnaJ-domain protein RME-8 functions in endosomal trafficking.
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pubmed:affiliation |
Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal QC H3A 2B4, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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