KCNE2 protein is more abundant in ventricles than in atria and can accelerate hERG protein degradation in a phosphorylation-dependent manner

American Journal of Physiology - Heart and Circulatory Physiology

Volumn 302, Issue 4, 2012, Pages

  Zhang, Mei ^a   Wang, Yuhong ^a   Jiang, Min ^a   Zankov, Dimitar P ^a   Chowdhury, Sabeeha ^a   Kasirajan, Vigneshwar ^a   Tseng, Gea Ny ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Cardiac electrophysiology; Long QT syndrome; Pulse chase experiments; Rapid delayed rectifier channel

Indexed keywords

ADENOVIRUS VECTOR; ANTIBODY; DELAYED RECTIFIER POTASSIUM CHANNEL; POTASSIUM CHANNEL HERG; POTASSIUM CHANNEL KCNE2;

AMPLITUDE MODULATION; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ANTIBODY DETECTION; ARTICLE; CELL SURFACE; CHANNEL GATING; CONTROLLED STUDY; GUINEA PIG; HEART ATRIUM; HEART MUSCLE CELL; HEART VENTRICLE; HUMAN; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY;

AMINO ACID SEQUENCE; ANIMALS; CELLS, CULTURED; DOGS; FEMALE; GUINEA PIGS; HEART ATRIA; HEART VENTRICLES; HUMANS; MALE; MODELS, ANIMAL; MOLECULAR SEQUENCE DATA; MYOCYTES, CARDIAC; PATCH-CLAMP TECHNIQUES; PHOSPHORYLATION; POTASSIUM CHANNELS, VOLTAGE-GATED; PROTEOLYSIS; RATS; RATS, INBRED SHR; SHAL POTASSIUM CHANNELS; TRANS-ACTIVATORS;

EID: 84863023479     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00691.2011     Document Type: Article

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