The Gβ 5 - RGS7 complex selectively inhibits muscarinic M3 receptor signaling via the interaction between the third intracellular loop of the receptor and the DEP domain of RGS7

Biochemistry

Volumn 48, Issue 10, 2009, Pages 2282-2289

  Sandiford, Simone L ^a   Slepak, Vladlen Z ^a  

^a UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COUPLED RECEPTORS; G PROTEINS; GTPASE-ACTIVATING PROTEINS; HETEROTRIMERIC G PROTEINS; IN-VITRO; MOLECULAR MECHANISMS; MUSCARINIC ACETYLCHOLINE RECEPTORS; MUSCARINIC RECEPTORS; RECEPTOR SIGNALING; REGULATORS OF G-PROTEIN SIGNALING; STRUCTURAL MOTIFS; THIRD INTRACELLULAR LOOPS;

AMINES; CALCIUM; OLIGOMERS; PROTEINS; SIGNAL TRANSDUCTION; SIGNALING;

DIELECTRIC DEVICES;

CHOLINERGIC RECEPTOR; DIMER; GONADORELIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HISTAMINE; HISTAMINE H1 RECEPTOR; MUSCARINIC M1 RECEPTOR; MUSCARINIC M3 RECEPTOR; MUSCARINIC M5 RECEPTOR; MUSCARINIC RECEPTOR; RECEPTOR SUBTYPE; RGS PROTEIN; CARBACHOL; CARRIER PROTEIN; GNB5 PROTEIN, HUMAN; PEPTIDE FRAGMENT; R7BP PROTEIN, HUMAN; RGS7 PROTEIN, HUMAN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BETA CHAIN; CALCIUM TRANSPORT; COMPLEX FORMATION; IN VITRO STUDY; MOBILIZATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN INTERACTION; PROTEIN MOTIF; SIGNAL TRANSDUCTION; ANIMAL; BRAIN; CALCIUM SIGNALING; CELL MEMBRANE; CHO CELL; CRICETULUS; CYTOSOL; DRUG ANTAGONISM; DRUG EFFECT; GENETIC TRANSFECTION; GENETICS; HAMSTER; HUMAN; METABOLISM; MUTATION; PHYSIOLOGY; PROTEIN BINDING;

ANIMALS; BRAIN; CALCIUM SIGNALING; CARBACHOL; CARRIER PROTEINS; CELL MEMBRANE; CHO CELLS; CRICETINAE; CRICETULUS; CYTOSOL; GTP-BINDING PROTEIN BETA SUBUNITS; HUMANS; MICE; MUTATION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; RECEPTOR, MUSCARINIC M3; RGS PROTEINS; SIGNAL TRANSDUCTION; TRANSFECTION;

EID: 64349091535     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801989c     Document Type: Article

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