Ubiquitination in the first cytoplasmic loop of μ-opioid receptors reveals a hierarchical mechanism of lysosomal down-regulation

Journal of Biological Chemistry

Volumn 286, Issue 46, 2011, Pages 40193-40204

  Hislop, James N ^a,b   Henry, Anastasia G ^b   Von Zastrows, Mark ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASMIC LOOPS; DOWN-REGULATION; ENDOSOMAL SORTING COMPLEX REQUIRED FOR TRANSPORTS; ENDOSOMES; HIERARCHICAL ORGANIZATIONS; HOMEOSTATIC REGULATIONS; ISOFORMS; NATURALLY OCCURRING; NEUROPEPTIDES; OPIOID DRUGS; OPIOID RECEPTORS; PROTEOLYTIC DEGRADATION; RADIOLIGAND BINDING; UBIQUITINATION;

BIOCHEMISTRY; BIOLOGY;

BIOLOGICAL MEMBRANES;

ESCRT PROTEIN; MU OPIATE RECEPTOR; RADIOLIGAND; UBIQUITIN;

ARTICLE; BINDING SITE; CELL COMPARTMENTALIZATION; CELL SELECTION; CONTROLLED STUDY; CYTOPLASM; DOWN REGULATION; ENDOCYTOSIS; HUMAN; HUMAN CELL; INTERNALIZATION; LIGAND BINDING; LYSOSOME; MULTIVESICULAR BODY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; UBIQUITINATION;

ANIMALS; DOWN-REGULATION; ENDOCYTOSIS; HEK293 CELLS; HUMANS; LYSOSOMES; MICE; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, OPIOID, MU; UBIQUITINATION;

EID: 81155126108     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.288555     Document Type: Article

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