title: Artificial phosphorylation sites modulate the activity of a voltage-gated potassium channel.
abstract: The KvAP potassium channel is representative of a family of voltage-gated ion channels where the membrane potential is sensed by a transmembrane helix containing several positively charged arginines. Previous work by Wang and Zocchi [A. Wang and G. Zocchi, PLoS ONE 6, e18598 (2011)] showed how a negatively charged polyelectrolyte attached in proximity to the voltage sensing element can bias the opening probability of the channel. Here we introduce three phosphorylation sites at the same location and show that the response curve of the channel shifts by about 20 mV upon phosphorylation, while other characteristics such as the single-channel conductance are unaffected. In summary, we construct an artificial phosphorylation site which confers allosteric regulation to the channel.
authors: Department of Physics and Astronomy, University of California Los Angeles, Los Angeles, California 90095-1547, USA.
authors: Amila
authors: A
authors: Ariyaratne
authors: Department of Physics and Astronomy, University of California Los Angeles, Los Angeles, California 90095-1547, USA.
authors: Giovanni
authors: G
authors: Zocchi
mesh_terms: D041522:Aeropyrum; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D055724:Electrophysiological Phenomena; D008958:Models, Molecular; D010766:Phosphorylation; D024642:Potassium Channels, Voltage-Gated / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D019843:Archaeal Proteins; D024642:Potassium Channels, Voltage-Gated