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Potassium Channels

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Cover of 'Potassium Channels'

Table of Contents

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    Book Overview
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    Chapter 1 Manipulating Potassium Channel Expression and Function in Hippocampal Neurons by In Utero Electroporation
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    Chapter 2 Studying KCNQ1 Mutation and Drug Response in Type 1 Long QT Syndrome Using Patient-Specific Induced Pluripotent Stem Cell-Derived Cardiomyocytes
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    Chapter 3 Monitoring Changes in the Abundance of Endogenously Expressed ATP-Sensitive Potassium (KATP) Channels in the Plasma Membrane Using Surface Biotinylation
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    Chapter 4 Nonsense-Mediated mRNA Decay of hERG Mutations in Long QT Syndrome
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    Chapter 5 Probing Subunits Interactions in KATP Channels Using Photo-Crosslinking via Genetically Encoded p-Azido-l-phenylalanine
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    Chapter 6 Hyper-SUMOylation of K+ Channels in Sudden Unexplained Death in Epilepsy: Isolation and Primary Culture of Dissociated Hippocampal Neurons from Newborn Mice for Subcellular Localization
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    Chapter 7 Simultaneous Real-Time Measurement of the β-Cell Membrane Potential and Ca2+ Influx to Assess the Role of Potassium Channels on β-Cell Function
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    Chapter 8 Methods for Characterizing Disease-Associated ATP-Sensitive Potassium Channel Mutations
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    Chapter 9 Thallium Flux Assay for Measuring the Activity of Monovalent Cation Channels and Transporters
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    Chapter 10 Nuclear Magnetic Resonance Approaches for Characterizing Protein-Protein Interactions
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    Chapter 11 Studying Mechanosensitivity of Two-Pore Domain K+ Channels in Cellular and Reconstituted Proteoliposome Membranes
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    Chapter 12 Migration of PIP2 on KCNQ2 Surface Revealed by Molecular Dynamics Simulations
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    Chapter 13 Studying Structural Dynamics of Potassium Channels by Single-Molecule FRET
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    Chapter 14 Patch-Clamp Recordings of the KcsA K+ Channel in Unilamellar Blisters
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    Chapter 15 Combinatorial Assembly of Lumitoxins
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    Chapter 16 Characterization of MC4R Regulation of the Kir7.1 Channel Using the Tl+ Flux Assay
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    Chapter 17 Stopped-Flow Fluorometric Ion Flux Assay for Ligand-Gated Ion Channel Studies
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    Chapter 18 In Vivo Analysis of Potassium Channelopathies: Loose Patch Recording of Purkinje Cell Firing in Living, Awake Zebrafish
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    Chapter 19 Site-Directed Unnatural Amino Acid Mutagenesis to Investigate Potassium Channel Pharmacology in Xenopus laevis Oocytes
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    Chapter 20 Random Spherically Constrained Single-Particle (RSC) Method to Study Voltage-Gated Ion Channels
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    Chapter 21 CW-EPR Spectroscopy and Site-Directed Spin Labeling to Study the Structural Dynamics of Ion Channels
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    Chapter 22 Ion Binding to Transport Proteins using Isothermal Titration Calorimetry
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    Chapter 23 Building Atomic Models of the Ion Channels Based on Low Resolution Electron Microscopy Maps and Homology Modeling
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    Chapter 24 Studying Kv Channels Function using Computational Methods
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    Chapter 25 Erratum to: Ion Binding to Transport Proteins using Isothermal Titration Calorimetry
Attention for Chapter 5: Probing Subunits Interactions in KATP Channels Using Photo-Crosslinking via Genetically Encoded p-Azido-l-phenylalanine
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Chapter title
Probing Subunits Interactions in KATP Channels Using Photo-Crosslinking via Genetically Encoded p-Azido-l-phenylalanine
Chapter number 5
Book title
Potassium Channels
Published in
Methods in molecular biology, January 2018
DOI 10.1007/978-1-4939-7362-0_5
Pubmed ID
Book ISBNs
978-1-4939-7361-3, 978-1-4939-7362-0
Authors

Prasanna Devaraneni, Emily A. Rex, Show-Ling Shyng

Abstract

Potassium channels are multimeric protein complexes regulated by diverse physiological and pharmacological ligands. The key to understanding mechanisms of channel regulation is the ability to detect structural changes associated with ligand binding. While high-resolution structural methods such as X-ray crystallography and single-particle cryo-electron microscopy offer direct visualization of channel structures, these methods do have limitations and may not be suitable for the question of interest. In this chapter, we describe the use of a photo-cross-linker unnatural amino acid, p-azido-L-phenylalanine, to probe interactions between two proteins, the sulfonylurea receptor 1 and the inwardly rectifying potassium channel Kir6.2, that form the ATP-sensitive potassium (KATP) channel complex in the absence or presence of ligands. The difference in the extent of crosslinking between a liganded state and unliganded state can be used as a readout of ligand-induced structural changes. We anticipate that the protocol described here will also be applicable for other potassium channels and protein complexes.

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Unknown 1 100%

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Readers by professional status Count As %
Student > Bachelor 1 100%
Readers by discipline Count As %
Chemistry 1 100%