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Journal of Neuroscience, Vol 15, 5486-5501, Copyright © 1995 by Society for Neuroscience
Thalamocortical projections have a K+ channel that is phosphorylated and modulated by cAMP-dependent protein kinase
H Moreno, C Kentros, E Bueno, M Weiser, A Hernandez, E Vega-Saenz de Miera, A Ponce, W Thornhill and B Rudy
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
The finding that some K+ channel mRNAs are restricted to certain
populations of neurons in the CNS suggests that there are K+ channels
tailored to certain neuronal circuits. One such example are the transcripts
from the KV3.2 gene, the majority of which are expressed in thalamic relay
neurons. To gain insights into the specific roles of KV3.2 subunits, site
specific antibodies were raised to determine their localization in thalamic
relay neurons. Immunohistochemical and focal lesioning studies demonstrate
that KV3.2 proteins are localized to the terminal fields of thalamocortical
projections. It is also shown that KV3.2 channels expressed in vitro are
strongly inhibited through phosphorylation by cAMP-dependent protein kinase
(PKA). Channels containing KV3.1 subunits, which otherwise exhibit nearly
identical electrophysiological properties in heterologous expression
systems but have a different and less restricted pattern of expression in
the CNS, are not affected by PKA. Therefore, this modulation might be
associated with the specific roles of KV3.2 subunits. Furthermore, we
demonstrate that KV3.2 proteins can be phosphorylated in situ by intrinsic
PKA. KV3.2 subunits display properties and have a localization consistent
with a role in the regulation of the efficacy of the thalamocortical
synapse, and could thereby participate in the neurotransmitter-mediated
control of functional states of the thalamocortical system associated with
global states of awareness.
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