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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2006-10-23
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pubmed:abstractText |
Receptor activity-modifying proteins (RAMPs) interact with and modify the behavior of the calcitonin receptor (CTR) and calcitonin receptor-like receptor (CLR). We have examined the contribution of the short intracellular C terminus, using constructs that delete the last eight amino acids of each RAMP. C-Terminal deletion of individual RAMPs had little effect on the signaling profile induced when complexed with CLR in COS-7 or human embryonic kidney (HEK)293 cells. Likewise, confocal microscopy revealed each of the mutant RAMPs translocated hemagglutinin-tagged CLR to the cell surface. In contrast, a pronounced effect of RAMP C-terminal truncation was seen for RAMP/CTRa complexes, studied in COS-7 cells, with significant attenuation of amylin receptor phenotype induction that was stronger for RAMP1 and -2 than RAMP3. The loss of amylin binding upon C-terminal deletion could be partially recovered with overexpression of Galpha(s), suggesting an impact of the RAMP C terminus on coupling of G proteins to the receptor complex. In HEK293 cells the c-Myc-RAMP1 C-terminal deletion mutant showed high receptor-independent cell surface expression; however, this construct showed low cell surface expression when expressed alone in COS-7 cells, indicating interaction of RAMPs with other cellular components via the C terminus. This mutant also had reduced cell surface expression when coexpressed with CTR. Thus, this study reveals important functionality of the RAMP C-terminal domain and identifies key differences in the role of the RAMP C terminus for CTR versus CLR-based receptors.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RAMP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RAMP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Activity-Modifying...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Activity-Modifying...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Activity-Modifying Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenomedullin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitonin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitonin Gene-Related...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Islet Amyloid Polypeptide,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0026-895X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1750-60
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16912219-Amino Acid Sequence,
pubmed-meshheading:16912219-Animals,
pubmed-meshheading:16912219-COS Cells,
pubmed-meshheading:16912219-Cercopithecus aethiops,
pubmed-meshheading:16912219-Cyclic AMP,
pubmed-meshheading:16912219-Epitopes,
pubmed-meshheading:16912219-GTP-Binding Protein alpha Subunits, Gs,
pubmed-meshheading:16912219-Humans,
pubmed-meshheading:16912219-Inhibitory Concentration 50,
pubmed-meshheading:16912219-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:16912219-Iodine Radioisotopes,
pubmed-meshheading:16912219-Membrane Proteins,
pubmed-meshheading:16912219-Molecular Sequence Data,
pubmed-meshheading:16912219-Mutant Proteins,
pubmed-meshheading:16912219-Phenotype,
pubmed-meshheading:16912219-Protein Binding,
pubmed-meshheading:16912219-Rats,
pubmed-meshheading:16912219-Receptor Activity-Modifying Protein 1,
pubmed-meshheading:16912219-Receptor Activity-Modifying Protein 3,
pubmed-meshheading:16912219-Receptor Activity-Modifying Proteins,
pubmed-meshheading:16912219-Receptors, Adrenomedullin,
pubmed-meshheading:16912219-Receptors, Calcitonin,
pubmed-meshheading:16912219-Receptors, Calcitonin Gene-Related Peptide,
pubmed-meshheading:16912219-Receptors, Islet Amyloid Polypeptide,
pubmed-meshheading:16912219-Receptors, Peptide,
pubmed-meshheading:16912219-Sequence Deletion,
pubmed-meshheading:16912219-Signal Transduction,
pubmed-meshheading:16912219-Structure-Activity Relationship,
pubmed-meshheading:16912219-Transfection
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pubmed:year |
2006
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pubmed:articleTitle |
A critical role for the short intracellular C terminus in receptor activity-modifying protein function.
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pubmed:affiliation |
Drug Discovery Biology Laboratory, Department of Pharmacology, Bldg. 13E, Monash University, Clayton, 3800 Victoria, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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