| The delta e13 isoform of the calcitonin receptor forms a six-transmembrane domain receptor with dominant-negative effects on receptor surface expression and signaling. | |
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MedLine Citation:
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PMID: 15860547 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The CTRdelta e13 splice variant of the rabbit calcitonin receptor, which lacks the 14 amino acids of the seventh transmembrane domain (TMD) that are encoded by exon 13, is poorly expressed on the cell surface, fails to mobilize intracellular calcium or activate Erk, and inhibits the cell surface expression of the full-length C1a isoform. Nuclear magnetic resonance- and fluorescence-activated cell sorter-based experiments showed that the residual seventh TMD of CTRdelta e13 fails to partition into the lipid bilayer, resulting in an extracellular C terminus. Truncating the receptor after residue 397 to delete the cytoplasmic tail resulted in reduced cell surface expression and an inability to mobilize intracellular calcium or activate Erk, but the truncated receptor did not inhibit C1a cell surface expression. In contrast, when the receptor was truncated after residue 374 to eliminate the entire seventh TMD domain and the C-terminal domain, the resulting receptor reduced the cell surface expression of C1a in a manner similar to that of CTRdelta e13. Thus, normal cell surface expression, mobilization of intracellular calcium, and Erk activation requires the cytoplasmic C-terminal tail of the CTR, whereas the absence of the seventh TMD in the transmembrane helical bundle causes the dominant-negative effect on the surface expression of C1a. |
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Authors:
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Thomas Seck; Maria Pellegrini; Ana Maria Florea; Veronique Grignoux; Roland Baron; Dale F Mierke; William C Horne |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. Date: 2005-04-28 |
Journal Detail:
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Title: Molecular endocrinology (Baltimore, Md.) Volume: 19 ISSN: 0888-8809 ISO Abbreviation: Mol. Endocrinol. Publication Date: 2005 Aug |
Date Detail:
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Created Date: 2005-07-25 Completed Date: 2005-12-02 Revised Date: 2011-09-26 |
Medline Journal Info:
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Nlm Unique ID: 8801431 Medline TA: Mol Endocrinol Country: United States |
Other Details:
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Languages: eng Pagination: 2132-44 Citation Subset: IM |
Affiliation:
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Yale University School of Medicine, Department of Orthopaedics, New Haven, Connecticut 06520, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Blotting, Western Calcium / metabolism Cell Line Cell Membrane / metabolism Cell Separation Cyclic AMP / metabolism Cytoplasm / metabolism DNA / metabolism Enzyme Activation Extracellular Signal-Regulated MAP Kinases / metabolism Flow Cytometry Genes, Dominant Humans Immunoprecipitation Magnetic Resonance Spectroscopy Peptides / chemistry Phosphorylation Protein Folding Protein Isoforms Protein Structure, Tertiary Rabbits Receptors, Calcitonin / chemistry*, metabolism Signal Transduction Temperature Transfection |
| Grant Support | |
ID/Acronym/Agency:
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AR-49879/AR/NIAMS NIH HHS; DE-04724/DE/NIDCR NIH HHS; GM-54083/GM/NIGMS NIH HHS; R01 AR049879-01/AR/NIAMS NIH HHS; R01 AR049879-02/AR/NIAMS NIH HHS; R01 AR057769-02/AR/NIAMS NIH HHS; R01 GM054082-08/GM/NIGMS NIH HHS; R01 GM054082-09/GM/NIGMS NIH HHS; R37 DE004724-24/DE/NIDCR NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Peptides; 0/Protein Isoforms; 0/Receptors, Calcitonin; 60-92-4/Cyclic AMP; 7440-70-2/Calcium; 9007-49-2/DNA; EC 2.7.11.24/Extracellular Signal-Regulated MAP Kinases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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