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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
Journal of Neuroscience 1 August 1995, 15 (8) 5486-5501; DOI: https://doi.org/10.1523/JNEUROSCI.15-08-05486.1995
H Moreno
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
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C Kentros
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
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E Bueno
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
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M Weiser
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
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A Hernandez
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
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E Vega-Saenz de Miera
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
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A Ponce
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
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W Thornhill
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
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B Rudy
Department of Physiology and Neuroscience, New York University Medical Center, New York 10016, USA.
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Abstract

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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The Journal of Neuroscience: 15 (8)
Journal of Neuroscience
Vol. 15, Issue 8
1 Aug 1995
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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, B Rudy
Journal of Neuroscience 1 August 1995, 15 (8) 5486-5501; DOI: 10.1523/JNEUROSCI.15-08-05486.1995

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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, B Rudy
Journal of Neuroscience 1 August 1995, 15 (8) 5486-5501; DOI: 10.1523/JNEUROSCI.15-08-05486.1995
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