IKs response to protein kinase A-dependent KCNQ1 phosphorylation requires direct interaction with microtubules

Cardiovascular Research

Volumn 79, Issue 3, 2008, Pages 427-435

  Nicolas, Céline S ^a,b,c   Park, Kyu Ho ^a,b,c,f   El Harchi, Aziza ^a,b,c,g   Camonis, Jacques ^d   Kass, Robert S ^e   Escande, Denis ^a,b,c   Mérot, Jean ^a,b,c   Loussouarn, Gildas ^a,b,c   Le Bouffant, Françoise ^a,b,c   Baró, Isabelle ^a,b,c  

^a L INSTITUT DU THORAX   (France)

^b CNRS   (France)

^c UNIVERSITÉ DE NANTES   (France)

^d INSTITUT CURIE   (France)

^e NewYork Presbyterian Hospital   (United States)

^f INSTITUTE FOR INTEGRATIVE BIOLOGY OF THE CELL I2BC   (France)

^g UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

tubulin; K+ channel; KCNQ1; Myocytes; PKA; Signal transduction

Indexed keywords

BETA TUBULIN; COLCHICINE; CYCLIC AMP DEPENDENT PROTEIN KINASE; PACLITAXEL; POTASSIUM CHANNEL KCNE1; POTASSIUM CHANNEL KCNQ1; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; KCNQ1 PROTEIN, HUMAN; TUBULIN; TUBULIN MODULATOR; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BIOSYNTHESIS; CELL STRAIN COS7; CONTROLLED STUDY; GUINEA PIG; HEART MUSCLE CELL; IMMUNOCYTOCHEMISTRY; IMMUNOPRECIPITATION; MICROTUBULE; NONHUMAN; OSMOSIS; PATCH CLAMP; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; TWO HYBRID SYSTEM; YEAST; ACTION POTENTIAL; ANIMAL; CELL STRAIN COS1; CERCOPITHECUS; DRUG EFFECT; ENZYMOLOGY; GENETIC TRANSFECTION; GENETICS; KINETICS; MALE; METABOLISM; MOUSE; OSMOTIC PRESSURE; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE;

A KINASE ANCHOR PROTEINS; ACTION POTENTIALS; ANIMALS; CERCOPITHECUS AETHIOPS; COS CELLS; CYCLIC AMP-DEPENDENT PROTEIN KINASES; GUINEA PIGS; KCNQ1 POTASSIUM CHANNEL; KINETICS; MALE; MICE; MICROTUBULES; MYOCYTES, CARDIAC; OSMOTIC PRESSURE; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; TRANSFECTION; TUBULIN; TUBULIN MODULATORS;

EID: 48749128550     PISSN: 00086363     EISSN: 17553245     Source Type: Journal    
DOI: 10.1093/cvr/cvn085     Document Type: Article

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