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• W2089334699 abstract "To identify regulators of the type 1A angiotensin II receptor (AT1A), we investigated the interaction of cellular proteins with a fusion protein containing the rat AT1A receptor carboxyl-terminus. An approximately 20 kDa cytoplasmic protein interacted with the fusion protein in a Ca2+-dependent manner and was identified as calmodulin. A control peptide with high affinity for Ca2+/calmodulin and a peptide corresponding to a membrane proximal portion of the AT1A receptor carboxyl-terminus with analogy to known calmodulin-binding sequences were synthesised and tested for calmodulin-binding. Using in vitro binding assays combined with gel shift analysis, we demonstrated the formation of complexes between calmodulin and both peptides, which were Ca2+-dependent and of 1:1 stoichiometry. Affinity gels produced from these peptides also purified calmodulin from cell extracts. These results suggest a novel feedback regulation of the AT1A receptor by Ca2+/calmodulin and identify the membrane proximal region of the carboxyl-terminus as a focal point for interactions important for AT1A receptor function." @default.
• W2089334699 created "2016-06-24" @default.
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• W2089334699 date "1999-07-23" @default.
• W2089334699 modified "2023-10-14" @default.
• W2089334699 title "Identification of a Ca²⁺/calmodulin-binding domain within the carboxyl-terminus of the angiotensin II (AT_1A) receptor" @default.
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• W2089334699 doi "https://doi.org/10.1016/s0014-5793(99)00904-7" @default.
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