RGSZ1, a G(z)-selective rgs protein in brain: Structure, membrane association, regulation by Gα(z) phosphorylation, and relationship to a G(z) gtpase-activating protein subfamily

Journal of Biological Chemistry

Volumn 273, Issue 40, 1998, Pages 26014-26025

  Wang, Jun ^a   Ducret, Axel ^b,c   Tu, Yaping ^a   Kozasa, Tohru ^a   Aebersold, Ruedi ^b   Ross, Elliott M ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

^c MERCK FROSST CENTRE FOR THERAPEUTIC RESEARCH   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; DETERGENT; GNAZ PROTEIN, HUMAN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; LIPOSOME; MEMBRANE PROTEIN; MESSENGER RNA; NERVE PROTEIN; PHOSPHOPROTEIN; PROTEIN; PROTEIN KINASE C; REGULATOR OF G PROTEIN SIGNALLING 19; REGULATOR OF G-PROTEIN SIGNALLING 19; RGS PROTEIN; RGS1 PROTEIN, HUMAN; RGS20 PROTEIN, HUMAN;

ANIMAL TISSUE; ARTICLE; ENZYME ACTIVATION; ENZYME PURIFICATION; ENZYME SUBSTRATE; GENE AMPLIFICATION; HYDROLYSIS; MEMBRANE BINDING; NONHUMAN; NUCLEOTIDE SEQUENCE; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN PHOSPHORYLATION; TARGET CELL; AMINO ACID SEQUENCE; ANIMAL; BRAIN; CATTLE; CHEMISTRY; DNA SEQUENCE; ENZYME SPECIFICITY; HUMAN; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PHOSPHORYLATION; PHYSIOLOGY; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BRAIN; CATTLE; CLONING, MOLECULAR; DETERGENTS; ENZYME ACTIVATION; GTP-BINDING PROTEIN ALPHA SUBUNITS; GTP-BINDING PROTEINS; GTPASE-ACTIVATING PROTEINS; HETEROTRIMERIC GTP-BINDING PROTEINS; HUMANS; LIPOSOMES; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN KINASE C; PROTEINS; RGS PROTEINS; RNA, MESSENGER; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 0032475515     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.40.26014     Document Type: Article

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