The glucagon-like peptide-2 receptor C terminus modulates β-arrestin-2 association but is dispensable for ligand-induced desensitization, endocytosis, and G-protein-dependent effector activation

Journal of Biological Chemistry

Volumn 280, Issue 23, 2005, Pages 22124-22134

  Estall, Jennifer L ^a,b   Koehler, Jacqueline A ^b   Yusta, Bernardo ^b   Drucker, Daniel J ^a,b,c  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c TORONTO GENERAL HOSPITAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; MOLECULAR STRUCTURE; MUTAGENS; POLYSACCHARIDES; SIGNALING; SURFACE PHENOMENA;

CELL SURFACE; MUTANTS; PEPTIDES; RECEPTORS;

ENZYME KINETICS;

BETA ARRESTIN; BETA ARRESTIN 2; CELL SURFACE RECEPTOR; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; G PROTEIN COUPLED RECEPTOR; GLUCAGON LIKE PEPTIDE 2 RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MUTANT PROTEIN; PROTEIN KINASE C; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DESENSITIZATION; ENDOCYTOSIS; ENZYME ACTIVATION; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; INTRACELLULAR TRANSPORT; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; RECEPTOR BINDING; RECEPTOR DOWN REGULATION; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; WESTERN BLOTTING;

ADENYLATE CYCLASE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; ARRESTINS; CELL CULTURE TECHNIQUES; CELL LINE, TUMOR; CELL MEMBRANE; CLATHRIN; CRICETINAE; CYCLIC AMP; DNA, COMPLEMENTARY; DOSE-RESPONSE RELATIONSHIP, DRUG; ENDOCYTOSIS; GTP-BINDING PROTEINS; HELA CELLS; HUMANS; KINETICS; LIGANDS; MEMBRANE MICRODOMAINS; MICROSCOPY, FLUORESCENCE; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHORYLATION; PLASMIDS; PROTEIN BINDING; PROTEIN KINASE C; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, GLUCAGON; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION; TIME FACTORS;

EID: 20444477139     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M500078200     Document Type: Article

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