期刊
MOLECULAR ENDOCRINOLOGY
卷 19, 期 8, 页码 2132-2144出版社
OXFORD UNIV PRESS INC
DOI: 10.1210/me.2004-0472
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资金
- NIAMS NIH HHS [R01 AR057769, R56 AR049879, R01 AR049879, AR-49879] Funding Source: Medline
- NIDCR NIH HHS [R01 DE004724, R37 DE004724, DE-04724] Funding Source: Medline
- NIGMS NIH HHS [GM-54083, R01 GM054082] Funding Source: Medline
The CTR Delta 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 CTR Delta 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 CTR Delta 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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