Differential phosphorylation provides a switch to control how α-arrestin Rod1 down-regulates mating pheromone response in saccharomyces cerevisiae

Genetics

Volumn 203, Issue 1, 2016, Pages 299-317

  Alvaro, Christopher G ^a   Aindow, Ann ^a,b   Thorner, Jeremy ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b HARVARD UNIVERSITY   (United States)

Author keywords

Adaptation; Desensitization; Down regulation; Endocytosis; Mating pheromone response

Indexed keywords

ADAPTOR PROTEIN; ALPHA ARRESTIN ROD1; CELL PROTEIN; CLATHRIN; FORMIN BNI1; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; PHEROMONE; RETINA S ANTIGEN; SERUM AND GLUCOCORTICOID REGULATED KINASE 1; STRESS ACTIVATED PROTEIN KINASE; UBIQUITIN LIGASE RSP5; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; CALCINEURIN; ESCRT PROTEIN; GLYCOGEN SYNTHASE KINASE 3; MATING HORMONE ALPHA FACTOR RECEPTOR; MCK1 PROTEIN, S CEREVISIAE; MEMBRANE PROTEIN; PROTEIN BINDING; PROTEIN SERINE THREONINE KINASE; ROD1 PROTEIN, S CEREVISIAE; RSP5 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SNF1-RELATED PROTEIN KINASES; STE2 PROTEIN, S CEREVISIAE;

ADAPTATION; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DOWN REGULATION; IN VITRO STUDY; IN VIVO STUDY; MATING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE; UBIQUITINATION; ASEXUAL REPRODUCTION; CHEMISTRY; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN DOMAIN; SIGNAL TRANSDUCTION;

ADAPTATION, BIOLOGICAL; CALCINEURIN; DOWN-REGULATION; ENDOSOMAL SORTING COMPLEXES REQUIRED FOR TRANSPORT; GLYCOGEN SYNTHASE KINASE 3; MEMBRANE PROTEINS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN-SERINE-THREONINE KINASES; RECEPTORS, MATING FACTOR; REPRODUCTION, ASEXUAL; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SIGNAL TRANSDUCTION; UBIQUITIN-PROTEIN LIGASE COMPLEXES;

EID: 84979943820     PISSN: 00166731     EISSN: 19432631     Source Type: Journal    
DOI: 10.1534/genetics.115.186122     Document Type: Article

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