Tuning the electrical properties of the heart by differential trafficking of KATP ion channel complexes.

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Title:	Tuning the electrical properties of the heart by differential trafficking of KATP ion channel complexes.
Authors:	林玉雯 Eric, C.Arakel Brandenburg, So¨ren Uchida, Keita Zhang, Haixia Lin, Yu-Wen Kohl, Tobias Schrul, Bianca Matthew, S.Sulkin Igor, R.Efimov Colin, G.Nichols Stephan, E.Lehnart Schwappach, Blanche
Contributors:	Department of Molecular Biology, Center for Biochemistry and Molecular Cell Biology Faculty of Life Sciences, University of Manchester Department of Cardiology & Pulmonology, Heart Research Center Göttingen, University Medicine Göttingen Department of Cell Biology and Physiology, and Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine Max-Planck Institute for Biophysical Chemistry Department of Biomedical Engineering, Washington University Center for Biomedical Engineering and Technology, University of Maryland Baltimore
Keywords:	ATP-sensitive K+ channels COPI KATP PKA Trafficking Protein kinase A Cardiomyocyte Coatomer Arg-based retrieval signal
Date:	2014-05
Issue Date:	2016-11-24T01:27:03Z (UTC)
Publisher:	UK:The Company of Biologists
Abstract:	The copy number of membrane proteins at the cell surface is tightly regulated. Many ion channels and receptors present retrieval motifs to COPI vesicle coats and are retained in the early secretory pathway. In some cases, the interaction with COPI is prevented by binding to 14-3-3 proteins. However, the functional significance of this antagonism between COPI and 14-3-3 in terminally differentiated cells is unknown. Here, we show that ATP-sensitive K(+) (KATP) channels, which are composed of Kir6.2 and SUR1 subunits, are stalled in the Golgi complex of ventricular, but not atrial, cardiomyocytes. Upon sustained β-adrenergic stimulation, which leads to activation of protein kinase A (PKA), SUR1-containing channels reach the plasma membrane of ventricular cells. We show that PKA-dependent phosphorylation of the C-terminus of Kir6.2 decreases binding to COPI and, thereby, silences the arginine-based retrieval signal. Thus, activation of the sympathetic nervous system releases this population of KATP channels from storage in the Golgi and, hence, might facilitate the adaptive response to metabolic challenges.
Relation:	Journal of cell science, 127(9), 2106-2119
Appears in Collections:	[生命科學系所] 期刊論文

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