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Internalization of the Hm1 muscarinic cholinergic receptor involves the third cytoplasmic loop
Author(s) -
Maeda Sadaaki,
Lameh Jelveh,
Mallet William G.,
Philip Mohan,
Ramachandran J.,
Sadée Wolfgang
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81199-x
Subject(s) - internalization , receptor , muscarinic acetylcholine receptor , muscarinic acetylcholine receptor m5 , microbiology and biotechnology , mutant , chemistry , amino acid , cytoplasm , enzyme linked receptor , agonist , muscarinic acetylcholine receptor m3 , biochemistry , biology , gene
The m1 muscarinic receptor was previously shown to stimulate phosphatidyl inositol (PI) turnover and to internalize rapidly upon agonist activation. Three receptor mutants with large deletions of the third cytoplasmic loop (i3) of human Hm1, leaving only 11 and 8 amino acids at the amino and carboxy terminal junctions of i3, respectively, retained full ability to stimulate PI turnover, when expressed in U293 cells, but receptor internalization was greatly reduced in two mutants with deletions reaching close to the NH 2 terminal of i3. We propose that a receptor domain located toward the amino terminal junction ofi3 plays a role in Hm1 internalization.