Protein kinase A activity controls the regulation of T-type Cav3.2 channels by Gβγ dimers

Journal of Biological Chemistry

Volumn 284, Issue 12, 2009, Pages 7465-7473

  Hu, Changlong ^a   DePuy, Seth D ^a   Yao, Junlan ^a   McIntire, William E ^a   Barrett, Paula Q ^a,b  

^a UNIVERSITY OF VIRGINIA   (United States)

^b NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL FUNCTIONS; CALCIUM CHANNELS; CATALYTIC ACTIVITY; CHANNEL ACTIVITY; CHANNEL CURRENTS; CHANNEL PORE; LOW VOLTAGES; MOLECULAR EVENTS; MOLECULAR SWITCHES; PROTEIN KINASE A; RECEPTOR ACTIVATION; REGULATORY MECHANISM; SELECTIVE CONCENTRATION; SERINE RESIDUES; TARGET ORGANS; TO EFFECT; WHOLE CELL;

AMINES; AMINO ACIDS; BRAIN; DIMERS; LAWS AND LEGISLATION;

CALCIUM;

ALDOSTERONE; CALCIUM CHANNEL T TYPE; CYCLIC AMP DEPENDENT PROTEIN KINASE; DOPAMINE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN BETA GAMMA DIMER; RECOMBINANT PROTEIN; SERINE; UNCLASSIFIED DRUG; VOLTAGE GATED CALCIUM CHANNEL; CACNA1H PROTEIN, HUMAN; DOPAMINE RECEPTOR STIMULATING AGENT; G PROTEIN BETA GAMMA; G-PROTEIN BETA GAMMA; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT;

ADRENAL CORTEX CARCINOMA; ARTICLE; CALCIUM CURRENT; CANCER CELL CULTURE; CELL STRAIN HEK293; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME REGULATION; HUMAN; HUMAN CELL; INHIBITION KINETICS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PHOSPHORYLATION; RECEPTOR UPREGULATION; ZONA GLOMERULOSA; AMINO ACID SUBSTITUTION; BIOSYNTHESIS; DIMERIZATION; DRUG EFFECT; GENETICS; METABOLISM; MISSENSE MUTATION; PHOSPHORYLATION; TUMOR CELL LINE;

ALDOSTERONE; AMINO ACID SUBSTITUTION; CALCIUM CHANNELS, T-TYPE; CELL LINE, TUMOR; CYCLIC AMP-DEPENDENT PROTEIN KINASES; DIMERIZATION; DOPAMINE; DOPAMINE AGONISTS; GTP-BINDING PROTEIN BETA SUBUNITS; GTP-BINDING PROTEIN GAMMA SUBUNITS; HUMANS; MUTATION, MISSENSE; PHOSPHORYLATION; ZONA GLOMERULOSA;

EID: 65549089013     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M808049200     Document Type: Article

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