TPC1 vacuole SV channel gains further shape – voltage priming of calcium-dependent gating |
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| Institution: | 1. Institute for Molecular Plant Physiology and Biophysics, University of Würzburg, Julius-von-Sachs Platz 2, 97082 Würzburg, Germany;1. International Genome Center, Jiangsu University, Zhenjiang 212013, China;2. State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Key Laboratory of Biotechnology in Plant Protection of Ministry of Agriculture and Zhejiang Province, Institute of Plant Virology, Ningbo University, Ningbo, China;1. Cell Biology, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany;2. Houji Laboratory in Shanxi Province, College of Agriculture, Shanxi Agricultural University, 030801 Taigu, China;3. Innovative Center of Molecular Genetics and Evolution, School of Life Sciences, Guangzhou University, 510006 Guangzhou, China;1. Shanghai Key Laboratory of Plant Molecular Sciences, College of Life Sciences, Shanghai Normal University, Shanghai 200234, China;1. Agricultural Biotechnology Division, National Institute for Biotechnology and Genetic Engineering (NIBGE), Constituent College of Pakistan Institute of Engineering and Applied Sciences, Jhang Road, Faisalabad, Pakistan;2. International Center for Chemical and Biological Sciences, University of Karachi, Karachi, Pakistan;1. Instituto de Hortofruticultura Subtropical y Mediterránea ‘La Mayora’ (IHSM-UMA-CSIC), Consejo Superior de Investigaciones Científicas, 29750 Algarrobo-Costa, Málaga, Spain;1. National Key Laboratory for Crop Genetics and Germplasm Enhancement and Utilization, Collaborative Innovation Center for Modern Crop Production Co-Sponsored by Province and Ministry (CIC-MCP), Nanjing Agricultural University, No.1 Weigang, Nanjing, Jiangsu 210095, China |
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| Abstract: | Across phyla, voltage-gated ion channels (VGICs) allow excitability. The vacuolar two-pore channel AtTPC1 from the tiny mustard plant Arabidopsis thaliana has emerged as a paradigm for deciphering the role of voltage and calcium signals in membrane excitation. Among the numerous experimentally determined structures of VGICs, AtTPC1 was the first to be revealed in a closed and resting state, fueling speculation about structural rearrangements during channel activation. Two independent reports on the structure of a partially opened AtTPC1 channel protein have led to working models that offer promising insights into the molecular switches associated with the gating process. We review new structure–function models and also discuss the evolutionary impact of two-pore channels (TPCs) on K+ homeostasis and vacuolar excitability. |
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