Mutating the dileucine motif of the human β2-adrenoceptor reduces the high initial rate of receptor phosphorylation by GRK without affecting postendocytic sorting

European Journal of Pharmacology

Volumn 635, Issue 1-3, 2010, Pages 9-15

  Awwad, Hibah O ^a,c   Millman, Ellen E ^b   Alpizar Foster, Estrella ^a   Moore, Robert H ^b   Knoll, Brian J ^a  

^a UNIVERSITY OF HOUSTON   (United States)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

^c UNIVERSITY OF OKLAHOMA COLLEGE OF PHARMACY   (United States)

Author keywords

2 adrenoceptor; Endocytosis; G protein coupled receptor kinase; Phosphorylation; Recycling; Sorting motif

Indexed keywords

ALANINE; BETA 2 ADRENERGIC RECEPTOR; G PROTEIN COUPLED RECEPTOR KINASE; SERINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CELL SELECTION; CELL STRAIN HEK293; CELL SURFACE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DILEUCINE MOTIF; ENDOCYTOSIS; HUMAN; HUMAN CELL; INTERNALIZATION; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; RECEPTOR DOWN REGULATION;

AMINO ACID MOTIFS; ANIMALS; CELL LINE; DOWN-REGULATION; ENDOCYTOSIS; G-PROTEIN-COUPLED RECEPTOR KINASES; HUMANS; KINETICS; LEUCINE; MUTANT PROTEINS; MUTATION; PHOSPHORYLATION; PROTEIN TRANSPORT; RECEPTORS, ADRENERGIC, BETA-2; SERINE;

EID: 77952319966     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejphar.2010.02.033     Document Type: Article

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