Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2005-4-25
pubmed:abstractText
Members of the RME-1/mRme-1/EHD1 protein family have recently been shown to function in the recycling of membrane proteins from recycling endosomes to the plasma membrane. RME-1 family proteins are normally found in close association with recycling endosomes and the vesicles and tubules emanating from these endosomes, consistent with the proposal that these proteins directly participate in endosomal transport. RME-1 family proteins contain a C-terminal EH (eps15 homology) domain thought to be involved in linking RME-1 to other endocytic proteins, a coiled-coil domain thought to be involved in homo-oligomerization and an N-terminal P-loop domain thought to mediate nucleotide binding. In the present study, we show that both Caenorhabditis elegans and mouse RME-1 proteins bind and hydrolyze ATP. No significant GTP binding or hydrolysis was detected. Mutation or deletion of the ATP-binding P-loop prevented RME-1 oligomerization and at the same time dissociated RME-1 from endosomes. In addition, ATP depletion caused RME-1 to lose its endosome association in the cell, resulting in cytosolic localization. Taken together, these results indicate that ATP binding is required for oligomerization of mRme-1/EHD1, which in turn is required for its association with endosomes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/EHD1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Ehd1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase, http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Nucleotides, http://linkedlifedata.com/resource/pubmed/chemical/RME-1 protein, C elegans, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17213-20
pubmed:dateRevised
2011-9-22
pubmed:meshHeading
pubmed-meshheading:15710626-Adenosine Triphosphatases, pubmed-meshheading:15710626-Adenosine Triphosphate, pubmed-meshheading:15710626-Animals, pubmed-meshheading:15710626-Blotting, Western, pubmed-meshheading:15710626-Caenorhabditis elegans, pubmed-meshheading:15710626-Caenorhabditis elegans Proteins, pubmed-meshheading:15710626-Cell Line, pubmed-meshheading:15710626-Cell Membrane, pubmed-meshheading:15710626-Cytosol, pubmed-meshheading:15710626-DNA, pubmed-meshheading:15710626-Endosomes, pubmed-meshheading:15710626-Escherichia coli, pubmed-meshheading:15710626-Gene Deletion, pubmed-meshheading:15710626-Glutathione Transferase, pubmed-meshheading:15710626-Green Fluorescent Proteins, pubmed-meshheading:15710626-Guanosine Triphosphate, pubmed-meshheading:15710626-HeLa Cells, pubmed-meshheading:15710626-Humans, pubmed-meshheading:15710626-Hydrolysis, pubmed-meshheading:15710626-Kinetics, pubmed-meshheading:15710626-Mice, pubmed-meshheading:15710626-Microscopy, Confocal, pubmed-meshheading:15710626-Microscopy, Fluorescence, pubmed-meshheading:15710626-Mutation, pubmed-meshheading:15710626-Nucleotides, pubmed-meshheading:15710626-Protein Binding, pubmed-meshheading:15710626-Protein Structure, Tertiary, pubmed-meshheading:15710626-Time Factors, pubmed-meshheading:15710626-Two-Hybrid System Techniques, pubmed-meshheading:15710626-Vesicular Transport Proteins
pubmed:year
2005
pubmed:articleTitle
ATP binding regulates oligomerization and endosome association of RME-1 family proteins.
pubmed:affiliation
Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural