Thalamocortical projections have a K+ channel that is phosphorylated and modulated by cAMP-dependent protein kinase
Cerebral Cortex
Male
0301 basic medicine
0303 health sciences
Potassium Channels
Molecular Sequence Data
Cyclic AMP-Dependent Protein Kinases
Immunohistochemistry
Synaptic Transmission
Rats
Electrophysiology
03 medical and health sciences
Thalamus
Cyclic AMP
Animals
Amino Acid Sequence
Phosphorylation
DOI:
10.1523/jneurosci.15-08-05486.1995
Publication Date:
2018-04-02T18:20:40Z
AUTHORS (9)
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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