Abstract

We investigated the role of the cytoplasmic tail of the thyrotropin receptor (TSHR) in signal transduction using mutants with truncation at the cytoplasmic tail. Mutant without residues 700-764 completely lost inositol phosphate response to agonists and showed decreased basal cAMP level. Mutant without residues 710-764 showed full cAMP responses but blunted inositol phosphate responses. However, mutant without residues 722-764 retained all signal transduction activities. These findings suggest that the amino-terminal half of the cytoplasmic tail (up to residue 721) is essential for full expression of functional activities.

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