ArticleMolecular endocrinology (Baltimore, Md.)2005
The delta e13 isoform of the calcitonin receptor forms a six-transmembrane domain receptor with dominant-negative effects on receptor surface expression and signaling.
Article in Molecular endocrinology (Baltimore, Md.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Key role of CRF in the skin stress response system.Endocrine reviews · 2013Review
- The roles played by highly truncated splice variants of G protein-coupled receptors.Journal of molecular signaling · 2012Article
- Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs?British journal of pharmacology · 2012Review
- Sensing the environment: regulation of local and global homeostasis by the skin's neuroendocrine system.Advances in anatomy, embryology, and cell biology · 2012Review
- Re-Evaluation of the PBAN Receptor Molecule: Characterization of PBANR Variants Expressed in the Pheromone Glands of Moths.Frontiers in endocrinology · 2012Article
- Expression and membrane topology of Anopheles gambiae odorant receptors in lepidopteran insect cells.PloS one · 2010Article
- Emerging role of alternative splicing of CRF1 receptor in CRF signaling.Acta biochimica Polonica · 2010Review
- Alternative splicing of G protein-coupled receptors: physiology and pathophysiology.Cellular and molecular life sciences : CMLS · 2009Review
- Calcitonin receptor plays a physiological role to protect against hypercalcemia in mice.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2008Article
- Secretin-receptor and secretin-receptor-variant expression in gastrinomas: correlation with clinical and tumoral features and secretin and calcium provocative test results.The Journal of clinical endocrinology and metabolism · 2007Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
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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