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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2006-4-21
pubmed:abstractText
CD39/ecto-NTPDase 1 (nucleoside triphosphate diphosphohydrolase 1) is an ecto-nucleotidase that influences P2 receptor activation to regulate vascular and immune cell adhesion and signalling events pivotal in inflammation. Whether CD39 interacts with other membrane or cytoplasmic proteins has not been established to date. Using the yeast two-hybrid system, we note that the N-terminus of CD39 binds to RanBPM (Ran binding protein M; also known as RanBP9), a multi-adaptor scaffolding membrane protein originally characterized as a binding protein for the small GTPase Ran. We confirm formation of complexes between CD39 and RanBPM in transfected mammalian cells by co-immunoprecipitation studies. Endogenous CD39 and RanBPM are also found to be co-expressed and abundant in cell membranes of B-lymphocytes. NTPDase activity of recombinant CD39, but not of N-terminus-deleted-CD39 mutant, is substantially diminished by RanBPM co-expression in COS-7 cells. The conserved SPRY [repeats in splA and RyR (ryanodine receptor)] moiety of RanBPM is insufficient alone for complete physical and functional interactions with CD39. We conclude that CD39 associations with RanBPM have the potential to regulate NTPDase catalytic activity. This intermolecular interaction may have important implications for the regulation of extracellular nucleotide-mediated signalling.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-10029517, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-10470077, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-10471369, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-10636909, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-10954728, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-10997340, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-11137554, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-11470507, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-11741967, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-11748109, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-11818027, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-12147692, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-12566920, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-14511641, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-14722085, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-15590415, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-15852225, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-3044186, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-7930580, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-8579614, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-8626624, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-8955160, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-8978031, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-9009824, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-9105634, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-9204703, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-9551996, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-9671706, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-9733785, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-9815100, http://linkedlifedata.com/resource/pubmed/commentcorrection/16478441-9817760
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1470-8728
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
396
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23-30
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:16478441-Adaptor Proteins, Signal Transducing, pubmed-meshheading:16478441-Animals, pubmed-meshheading:16478441-Antigens, CD, pubmed-meshheading:16478441-Apyrase, pubmed-meshheading:16478441-B-Lymphocytes, pubmed-meshheading:16478441-COS Cells, pubmed-meshheading:16478441-Cell Line, Transformed, pubmed-meshheading:16478441-Cell Membrane, pubmed-meshheading:16478441-Cercopithecus aethiops, pubmed-meshheading:16478441-Cytoskeletal Proteins, pubmed-meshheading:16478441-DNA, Complementary, pubmed-meshheading:16478441-Humans, pubmed-meshheading:16478441-Mice, pubmed-meshheading:16478441-Nuclear Proteins, pubmed-meshheading:16478441-Protein Binding, pubmed-meshheading:16478441-Protein Interaction Mapping, pubmed-meshheading:16478441-Protein Structure, Tertiary, pubmed-meshheading:16478441-Recombinant Fusion Proteins, pubmed-meshheading:16478441-Structure-Activity Relationship, pubmed-meshheading:16478441-Transfection, pubmed-meshheading:16478441-Two-Hybrid System Techniques, pubmed-meshheading:16478441-ran GTP-Binding Protein
pubmed:year
2006
pubmed:articleTitle
RanBPM associates with CD39 and modulates ecto-nucleotidase activity.
pubmed:affiliation
Liver Center, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.
pubmed:publicationType
Journal Article
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