Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-6-4
pubmed:abstractText
RME-1 is an Eps15-homology (EH)-domain protein that was identified in a genetic screen for endocytosis genes in Caenorhabditis elegans. When expressed in a CHO cell line, the worm RME-1 protein and a mouse homologue are both associated with the endocytic recycling compartment. Here we show that expression of a dominant-negative construct with a point mutation near the EH domain results in redistribution of the endocytic recycling compartment and slowing down of transferrin receptor recycling. The delivery of a TGN38 chimaeric protein to the trans-Golgi network is also slowed down. The function of Rme-1 in endocytic recycling is evolutionarily conserved in metazoans as shown by the protein's properties in C. elegans.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Eps15 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Furin, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Subtilisins, http://linkedlifedata.com/resource/pubmed/chemical/Tgoln1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Tgoln2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Transferrin
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1465-7392
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
567-72
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11389441-Animals, pubmed-meshheading:11389441-CHO Cells, pubmed-meshheading:11389441-Caenorhabditis elegans Proteins, pubmed-meshheading:11389441-Calcium-Binding Proteins, pubmed-meshheading:11389441-Cell Compartmentation, pubmed-meshheading:11389441-Cricetinae, pubmed-meshheading:11389441-Furin, pubmed-meshheading:11389441-Glycoproteins, pubmed-meshheading:11389441-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:11389441-Membrane Glycoproteins, pubmed-meshheading:11389441-Membrane Proteins, pubmed-meshheading:11389441-Mice, pubmed-meshheading:11389441-Mutation, pubmed-meshheading:11389441-Phosphoproteins, pubmed-meshheading:11389441-Protein Structure, Tertiary, pubmed-meshheading:11389441-Subtilisins, pubmed-meshheading:11389441-Transferrin, pubmed-meshheading:11389441-Transport Vesicles
pubmed:year
2001
pubmed:articleTitle
Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells.
pubmed:affiliation
Department of Biochemistry, Weill Medical College of Cornell University, 1300 York Avenue, New York, New York 10021, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't