|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
9
|
|
pubmed:dateCreated |
2005-2-28
|
|
pubmed:abstractText |
In mice genetic ablation of expression of either melanin-concentrating hormone or the melanin-concentrating hormone-1 receptor results in alterations in energy metabolism and a lean phenotype. There is thus great interest in the function and regulation of this receptor. Using the yeast two-hybrid system we identified an interaction of the actin- and intermediate filament-binding protein periplakin with the intracellular C-terminal tail of the melanin-concentrating hormone-1 receptor. Direct association of these proteins was verified in pull-down and coimmunoprecipitation experiments. Truncations and internal deletions delineated the site of interaction to a group of 11 amino acids proximal to transmembrane helix VII, which was distinct from the binding site for the melanin-concentrating hormone-1 receptor-interacting zinc finger protein. Immunohistochemistry demonstrated coexpression of periplakin with melanin-concentrating hormone-1 receptor in specific cells of the piriform cortex, amygdala, and other structures of the adult mouse brain. Coexpression of the melanin-concentrating hormone-1 receptor with periplakin in human embryonic kidney 293 cells did not prevent agonist-mediated internalization of the receptor but did interfere with binding of (35)S-labeled guanosine 5'-3-O-(thio)triphosphate ([(35)S]GTPgammaS) to the G protein Galpha(o1) and the elevation of [Ca(2+)](i). Coexpression of the receptor with the interacting zinc finger protein did not modulate receptor internalization or G protein activation. The interaction of periplakin with receptors was selective. Coexpression of periplakin with the IP prostanoid receptor did not result in coimmunoprecipitation nor interfere with agonist-mediated binding of [(35)S]GTPgammaS to the G protein Galpha(s). Periplakin is the first protein described to modify the capacity of the melanin-concentrating hormone-1 receptor to initiate signal transduction.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Biotin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Signal-Regulated MAP...,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/MCHR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Plakins,
http://linkedlifedata.com/resource/pubmed/chemical/Ppl protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Somatostatin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
4
|
|
pubmed:volume |
280
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
8208-20
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:15590649-Actins,
pubmed-meshheading:15590649-Amino Acid Sequence,
pubmed-meshheading:15590649-Animals,
pubmed-meshheading:15590649-Binding Sites,
pubmed-meshheading:15590649-Biotin,
pubmed-meshheading:15590649-Brain,
pubmed-meshheading:15590649-Calcium,
pubmed-meshheading:15590649-Cell Line,
pubmed-meshheading:15590649-Cell Membrane,
pubmed-meshheading:15590649-Cytoskeletal Proteins,
pubmed-meshheading:15590649-DNA,
pubmed-meshheading:15590649-DNA, Complementary,
pubmed-meshheading:15590649-Dose-Response Relationship, Drug,
pubmed-meshheading:15590649-Extracellular Signal-Regulated MAP Kinases,
pubmed-meshheading:15590649-GTP-Binding Proteins,
pubmed-meshheading:15590649-Gene Library,
pubmed-meshheading:15590649-Glutathione Transferase,
pubmed-meshheading:15590649-Green Fluorescent Proteins,
pubmed-meshheading:15590649-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:15590649-Histidine,
pubmed-meshheading:15590649-Humans,
pubmed-meshheading:15590649-Immunoblotting,
pubmed-meshheading:15590649-Immunohistochemistry,
pubmed-meshheading:15590649-Immunoprecipitation,
pubmed-meshheading:15590649-Mice,
pubmed-meshheading:15590649-Microscopy, Confocal,
pubmed-meshheading:15590649-Microscopy, Fluorescence,
pubmed-meshheading:15590649-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:15590649-Molecular Sequence Data,
pubmed-meshheading:15590649-Phenotype,
pubmed-meshheading:15590649-Phosphorylation,
pubmed-meshheading:15590649-Plakins,
pubmed-meshheading:15590649-Plasmids,
pubmed-meshheading:15590649-Protein Binding,
pubmed-meshheading:15590649-Protein Structure, Tertiary,
pubmed-meshheading:15590649-RNA,
pubmed-meshheading:15590649-RNA, Messenger,
pubmed-meshheading:15590649-Rats,
pubmed-meshheading:15590649-Receptors, Somatostatin,
pubmed-meshheading:15590649-Recombinant Fusion Proteins,
pubmed-meshheading:15590649-Signal Transduction,
pubmed-meshheading:15590649-Time Factors,
pubmed-meshheading:15590649-Transfection,
pubmed-meshheading:15590649-Two-Hybrid System Techniques,
pubmed-meshheading:15590649-Zinc Fingers
|
|
pubmed:year |
2005
|
