Role of β-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking

Current Opinion in Cell Biology

Volumn 27, Issue 1, 2014, Pages 63-71

  Kang, Dong Soo ^a   Tian, Xufan ^a   Benovic, Jeffrey L ^a  

^a THOMAS JEFFERSON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 6; ALPHA ARRESTIN; ARRESTIN DOMAIN CONTAINING PROTEIN; BETA 2 ADAPTIN; BETA 2 ADRENERGIC RECEPTOR; BETA ADAPTIN; BETA ARRESTIN; BETA ARRESTIN 1; CHEMOKINE RECEPTOR CXCR4; CLATHRIN; ENDOTHELIAL NITRIC OXIDE SYNTHASE; ESCRT PROTEIN; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; MU 2 ADAPTIN; MU ADAPTIN; PARKIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOPEPTIDE; PROTEIN MDM2; RETINA S ANTIGEN; TRANSCRIPTION FACTOR AP 2; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG; UNINDEXED DRUG; VASOPRESSIN V2 RECEPTOR; VPS26 PROTEIN; PROTEIN BINDING;

AMINO TERMINAL SEQUENCE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELLULAR DISTRIBUTION; CRYSTAL STRUCTURE; ENDOCYTOSIS; ENDOSOME; EUKARYOTE; INTERNALIZATION; MAMMAL; MOLECULAR DYNAMICS; NITROSYLATION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DEPHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TRANSPORT; REVIEW; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION; SUMOYLATION; UBIQUITINATION; WILD TYPE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; PHOSPHORYLATION; PROTEIN TERTIARY STRUCTURE;

ANIMALS; ARRESTINS; ENDOCYTOSIS; HUMANS; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECEPTORS, G-PROTEIN-COUPLED; SIGNAL TRANSDUCTION;

EID: 84890157678     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2013.11.005     Document Type: Review

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