Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 102, Issue 49, Pages 17828-17833Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0509122102
Keywords
KCNQ; M-channel; S4-S5 loop; potassium channels; neuromodulation
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Funding
- NCRR NIH HHS [RR01614, RR14606, P41 RR001614] Funding Source: Medline
- NIMH NIH HHS [R01 MH065334, MH65334] Funding Source: Medline
- NINDS NIH HHS [R21 NS042100, R21 NS42100] Funding Source: Medline
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Neuronal potassium channel subunits of the KCNQ (Kv7) family underlie M-current (I-M), and may also underlie the slow potassium current at the node of Ranvier, I-Ks. I-M and I-Ks, are outwardly rectifying currents that regulate excitability of neurons and myelinated axons, respectively. Studies of native I-M and heterologously expressed Kv7 subunits suggest that, in vivo, KCNQ channels exist within heterogeneous, multicomponent protein complexes. KCNQ channel properties are regulated by protein phosphorylation, protein-protein interactions, and protein-lipid interactions within such complexes. To better understand the regulation of neuronal KCNQ channels, we searched directly for posttranslational modificationson KCNQ2/KCNQ3 channels in vivo by using mass spectrometry. Here we describe two sites of phosphorylation. One site, specific for KCNQ3, appears functionally silent in electrophysiological assays but is located in a domain previously shown to be important for subunit tetramerization. Mutagenesis and electrophysiological studies of the second site, located in the S4-S5 intracellular loop of all KCNQ subunits, reveal a mechanism of channel inhibition.
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