Palmitoylation of muscarinic acetylcholine receptor m2 subtypes: Reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail

Archives of Biochemistry and Biophysics

Volumn 340, Issue 2, 1997, Pages 376-382

  Hayashi, Mariko Kato ^a   Haga, Tatsuya ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

acetylcholine; G protein; muscarinic; palmitoylation; phosphorylation

Indexed keywords

ALANINE; CYSTEINE; GUANINE NUCLEOTIDE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE; MUSCARINIC M2 RECEPTOR; PALMITIC ACID; PHOSPHOLIPID; PHOSPHOTRANSFERASE; RECEPTOR SUBTYPE;

ANIMAL CELL; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; LEPIDOPTERA; MUTATION; NONHUMAN; PALMITOYLATION; PHOSPHOLIPID VESICLE; PHOSPHORYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STOP CODON;

EID: 0031569809     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1006/abbi.1997.9906     Document Type: Article

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