Heterodimerization of V1a and V2 vasopressin receptors determines the interaction with β-arrestin and their trafficking patterns

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 6, 2004, Pages 1548-1553

  Terrillon, Sonia ^a,b   Barberis, Claude ^b   Bouvier, Michel ^a,c  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

^b INSERM   (France)

^c UNIVERSITY OF MONTREAL   (Canada)

Author keywords

Endosomes; G protein coupled receptors; Internalization; Oligomerization; Recycling

Indexed keywords

BETA ARRESTIN; HORMONE RECEPTOR STIMULATING AGENT; MUTANT PROTEIN; UNCLASSIFIED DRUG; VASOPRESSIN RECEPTOR STIMULATING AGENT; VASOPRESSIN V1 RECEPTOR; VASOPRESSIN V1 RECEPTOR STIMULATING AGENT; VASOPRESSIN V2 RECEPTOR; VASOPRESSIN V2 RECEPTOR STIMUALTING AGENT;

ARTICLE; CELL MEMBRANE; CELL SURFACE; DIMERIZATION; DRUG SELECTIVITY; EMBRYO; ENDOCYTOSIS; ENDOSOME; HUMAN; HUMAN CELL; MEMBRANE TRANSPORT; MEMBRANE VESICLE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TRANSPORT;

ARRESTINS; CELL LINE; DIMERIZATION; ENDOCYTOSIS; HUMANS; MICROSCOPY, FLUORESCENCE; PROTEIN TRANSPORT; RECEPTORS, VASOPRESSIN;

EID: 1242274647     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0305322101     Document Type: Article

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