14-3-3θ is a binding partner of rat eag1 potassium channels14-3-3θ鼠eag1钾离子通道是具有约束力的合作伙伴.pdfVIP

14-3-3θ is a binding partner of rat eag1 potassium channels14-3-3θ鼠eag1钾离子通道是具有约束力的合作伙伴.pdf

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14-3-3θ is a binding partner of rat eag1 potassium channels14-3-3θ鼠eag1钾离子通道是具有约束力的合作伙伴

14-3-3h is a Binding Partner of Rat Eag1 Potassium Channels 1¤ 3 1¤ 1 1¤ 4 Po-Hao Hsu , Shi-Chuen Miaw , Chau-Ching Chuang , Pei-Yu Chang , Ssu-Ju Fu , Guey-Mei Jow , Mei-Miao Chiu1, Chung-Jiuan Jeng1,2* 1 Institute of Anatomy and Cell Biology, School of Medicine, National Yang-Ming University, Taipei, Taiwan, 2 Brain Research Center, National Yang-Ming University, Taipei, Taiwan, 3 Graduate Institute of Immunology, College of Medicine, National Taiwan University, Taipei, Taiwan, 4 School of Medicine, Fu-Jen Catholic University, Hsin- Chuang, New Taipei City, Taiwan Abstract ` + + The ether-a-go-go (Eag) potassium (K ) channel belongs to the superfamily of voltage-gated K channel. In mammals, the expression of Eag channels is neuron-specific but their neurophysiological role remains obscure. We have applied the yeast two-hybrid screening system to identify rat Eag1 (rEag1)-interacting proteins from a rat brain cDNA library. One of the clones we identified was 14-3-3h, which belongs to a family of small acidic protein abundantly expressed in the brain. Data from in vitro yeast two-hybrid and GST pull-down assays suggested that the direct association with 14-3-3h was mediated by both the N- and the C-termini of rEag1. Co-precipitation of the two proteins was confirmed in both heterologous HEK293T cells and native hippocampal neurons. Electrophysiological studies showed that over-expression of 14-3-3h led to a sizable suppression of rEag1 K+ currents with no apparent alteration of the steady-state voltage d

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