Source:http://linkedlifedata.com/resource/pubmed/id/12107182
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
37
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pubmed:dateCreated |
2002-9-9
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pubmed:abstractText |
The binding of extracellular ATP to the P2X(7) receptor opens an integral cation-permeable channel; it also leads to membrane blebbing and, in certain immune cells, interleukin-1beta secretion and eventual death. The latter three effects are unique to the P2X(7) receptor; also unique among P2X receptors is the long intracellular C terminus of the protein. We have shown that the C-terminal domain of the P2X(7) receptor is responsible for the cell blebbing phenotype. A screen for proteins that associate with the C-terminal domain of the P2X(7) receptor and might mediate the blebbing phenotype, identified epithelial membrane protein 2 (EMP-2). The interaction between EMP-2 and P2X(7) was confirmed biochemically by co-immunoprecipitation, co-purification, and glutathione S-transferase pull-down assays, and this interaction was entirely dependent on the C-terminal domain of P2X(7). The P2X(7) receptor also interacted with the other members of the epithelial membrane protein family (EMP-1, EMP-3, and PMP-22). All four EMPs were found to be expressed in HEK-293 cells and in THP-1 monocytes, which express P2X(7) receptors. Interestingly, the constitutive overexpression of any of the EMPs in HEK-293 cells led to cell blebbing, annexin V binding, and cell death, by a caspase-dependent pathway. These findings suggest that the P2X(7) C-terminal domain associates with EMPs, and this interaction may mediate some aspects of the downstream signaling following P2X(7) receptor activation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/EMP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/P2RX7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/P2rx7 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/PMP22 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Pmp22 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2X7
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
34017-23
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12107182-Amino Acid Sequence,
pubmed-meshheading:12107182-Apoptosis,
pubmed-meshheading:12107182-Cell Line,
pubmed-meshheading:12107182-Cell Membrane,
pubmed-meshheading:12107182-Humans,
pubmed-meshheading:12107182-Membrane Glycoproteins,
pubmed-meshheading:12107182-Membrane Proteins,
pubmed-meshheading:12107182-Molecular Sequence Data,
pubmed-meshheading:12107182-Myelin Proteins,
pubmed-meshheading:12107182-Precipitin Tests,
pubmed-meshheading:12107182-Receptors, Purinergic P2,
pubmed-meshheading:12107182-Receptors, Purinergic P2X7
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pubmed:year |
2002
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pubmed:articleTitle |
Epithelial membrane proteins induce membrane blebbing and interact with the P2X7 receptor C terminus.
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pubmed:affiliation |
Institute of Molecular Physiology, University of Sheffield S10 2TN, United Kingdom. H.L.Wilson@sheffield.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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