Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding

Cellular Signalling

Volumn 25, Issue 11, 2013, Pages 2155-2162

  Vishnivetskiy, Sergey A ^a   Ostermaier, Martin K ^b   Singhal, Ankita ^b   Panneels, Valerie ^b   Homan, Kristoff T ^c   Glukhova, Alisa ^c   Sligar, Stephen G ^d   Tesmer, John J G ^c   Schertler, Gebhard F X ^b,e   Standfuss, Joerg ^b   Gurevich, Vsevolod V ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b PAUL SCHERRER INSTITUTE   (Switzerland)

^c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^d UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^e ETH ZURICH   (Switzerland)

Author keywords

Arrestin; GPCR; GRK; Monomer; Nanodiscs; Phosphorylation

Indexed keywords

ARRESTIN 1 PROTEIN; BINDING PROTEIN; G PROTEIN COUPLED RECEPTOR KINASE 2; G PROTEIN COUPLED RECEPTOR KINASE 5; HIGH DENSITY LIPOPROTEIN; MUTANT PROTEIN; RHODOPSIN; RHODOPSIN KINASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; NIGHT BLINDNESS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; SIGNAL TRANSDUCTION; WILD TYPE;

ARRESTIN; DARK PHOSPHORYLATED RHODOPSIN; DARK UNPHOSPHORYLATED RHODOPSIN; G PROTEIN-COUPLED RECEPTOR; G PROTEIN-COUPLED RECEPTOR KINASE; GPCR; GRK; LIGHT-ACTIVATED PHOSPHORYLATED RHODOPSIN; LIGHT-ACTIVATED UNPHOSPHORYLATED RHODOPSIN; MONOMER; NANODISCS; P-OPS; P-RH; P-RH*; PHOSPHO-OPSIN; PHOSPHORYLATION; RH; RH*; WILD TYPE; WT;

ANIMALS; ARRESTIN; CATTLE; CHOLESTEROL, HDL; G-PROTEIN-COUPLED RECEPTOR KINASE 1; GENE EXPRESSION REGULATION; ISOENZYMES; MUTATION; NIGHT BLINDNESS; OPSINS; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN MULTIMERIZATION; RETINAL ROD PHOTORECEPTOR CELLS; RHODOPSIN; SIGNAL TRANSDUCTION;

EID: 84881111811     PISSN: 08986568     EISSN: 18733913     Source Type: Journal    
DOI: 10.1016/j.cellsig.2013.07.009     Document Type: Article

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