VAMP2 interacts directly with the N terminus of Kv2.1 to enhance channel inactivation

Pflugers Archiv European Journal of Physiology

Volumn 456, Issue 6, 2008, Pages 1121-1136

  Lvov, Anatoli ^a   Chikvashvili, Dodo ^a   Michaelevski, Izhak ^b   Lotan, Ilana ^a  

^a TEL AVIV UNIVERSITY   (Israel)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Inactivation; Kv2.1; T1 domain; VAMP2

Indexed keywords

MUTANT PROTEIN; POTASSIUM CHANNEL KV1.5; SYNAPTOBREVIN 2; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL; VOLTAGE GATED POTASSIUM CHANNEL KV2.1;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BIOCHEMISTRY; BRAIN MEMBRANE; CELL MEMBRANE; CONTROLLED STUDY; ELECTROPHYSIOLOGY; IN VITRO STUDY; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; RAT; WILD TYPE; XENOPUS;

ANIMALS; BLOTTING, WESTERN; BRAIN CHEMISTRY; CELL MEMBRANE; ELECTROPHYSIOLOGY; GLUTATHIONE TRANSFERASE; IMMUNOPRECIPITATION; KINETICS; MODELS, MOLECULAR; OOCYTES; PATCH-CLAMP TECHNIQUES; RATS; SHAB POTASSIUM CHANNELS; VESICLE-ASSOCIATED MEMBRANE PROTEIN 2; XENOPUS LAEVIS;

EID: 50049100089     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-008-0468-7     Document Type: Article

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