The nature of the arrestin·receptor complex determines the ultimate fate of the internalized receptor

Journal of Biological Chemistry

Volumn 278, Issue 13, 2003, Pages 11623-11632

  Pan, Ling ^b   Gurevich, Eugenia V ^b   Gurevich, Vsevolod V ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANES; PLASMAS; PROTEINS;

PHOSPHORYLATION;

BIOCHEMISTRY;

ARRESTIN 2; BETA 2 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR STIMULATING AGENT; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR KINASE; MUTANT PROTEIN; RECEPTOR; RETINA S ANTIGEN; UNCLASSIFIED DRUG; BETA ADRENERGIC RECEPTOR KINASE; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; CELL SURFACE RECEPTOR; CYCLIC AMP DEPENDENT PROTEIN KINASE;

ARTICLE; BINDING AFFINITY; CELL MEMBRANE; CONTROLLED STUDY; EMBRYO; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; INTERNALIZATION; LYSOSOME; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN TARGETING; RECEPTOR BINDING; RECEPTOR DOWN REGULATION; CELL LINE; CONFOCAL MICROSCOPY; DOWN REGULATION; DRUG EFFECT; DRUG POTENTIATION; ENDOCYTOSIS; METABOLISM; PHOSPHORYLATION; WESTERN BLOTTING;

ADRENERGIC BETA-AGONISTS; ARRESTIN; BETA-ADRENERGIC RECEPTOR KINASE; BLOTTING, WESTERN; CELL LINE; CYCLIC AMP-DEPENDENT PROTEIN KINASES; DOWN-REGULATION; ENDOCYTOSIS; HUMANS; MICROSCOPY, CONFOCAL; PHOSPHORYLATION; RECEPTORS, ADRENERGIC, BETA-2; RECEPTORS, CELL SURFACE;

EID: 0037838870     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M209532200     Document Type: Article

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