Skip to main content
construction release_alert
Profile editing will be unavailable for Scholars@Duke profiles from June 11-24, 2026 as manual profile data entry transitions to Elements. More information about the transition.
cancel

A C-terminal domain directs Kv3.3 channels to dendrites.

Publication ,  Journal Article
Deng, Q; Rashid, AJ; Fernandez, FR; Turner, RW; Maler, L; Dunn, RJ
Published in: J Neurosci
December 14, 2005

Pyramidal neurons of the electrosensory lateral line lobe (ELL) of Apteronotus leptorhynchus express Kv3-type voltage-gated potassium channels that give rise to high-threshold currents at the somatic and dendritic levels. Two members of the Kv3 channel family, AptKv3.1 and AptKv3.3, are coexpressed in these neurons. AptKv3.3 channels are expressed at uniformly high levels in each of four ELL segments, whereas AptKv3.1 channels appear to be expressed in a graded manner with higher levels of expression in segments that process high-frequency electrosensory signals. Immunohistochemical and recombinant channel expression studies show a differential distribution of these two channels in the dendrites of ELL pyramidal neurons. AptKv3.1 is concentrated in somas and proximal dendrites, whereas AptKv3.3 is distributed throughout the full extent of the large dendritic tree. Recombinant channel expression of AptKv3 channels through in vivo viral injections allowed directed retargeting of AptKv3 subtypes over the somadendritic axis, revealing that the sequence responsible for targeting channels to distal dendrites lies within the C-terminal domain of the AptKv3.3 protein. The targeting domain includes a consensus sequence predicted to bind to a PDZ (postsynaptic density-95/Discs large/zona occludens-1)-type protein-protein interaction motif. These findings reveal that different functional roles for Kv3 potassium channels at the somatic and dendritic level of a sensory neuron are attained through specific targeting that selectively distributes Kv3.3 channels to the dendritic compartment.

Duke Scholars

Published In

J Neurosci

DOI

EISSN

1529-2401

Publication Date

December 14, 2005

Volume

25

Issue

50

Start / End Page

11531 / 11541

Location

United States

Related Subject Headings

  • Shaw Potassium Channels
  • Rats
  • Protein Structure, Tertiary
  • Peptide Fragments
  • Neurons, Afferent
  • Neurology & Neurosurgery
  • Molecular Sequence Data
  • Mice
  • Gymnotiformes
  • Fish Proteins
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Deng, Q., Rashid, A. J., Fernandez, F. R., Turner, R. W., Maler, L., & Dunn, R. J. (2005). A C-terminal domain directs Kv3.3 channels to dendrites. J Neurosci, 25(50), 11531–11541. https://doi.org/10.1523/JNEUROSCI.3672-05.2005
Deng, Qingwei, Asim J. Rashid, Fernando R. Fernandez, Ray W. Turner, Leonard Maler, and Robert J. Dunn. “A C-terminal domain directs Kv3.3 channels to dendrites.J Neurosci 25, no. 50 (December 14, 2005): 11531–41. https://doi.org/10.1523/JNEUROSCI.3672-05.2005.
Deng Q, Rashid AJ, Fernandez FR, Turner RW, Maler L, Dunn RJ. A C-terminal domain directs Kv3.3 channels to dendrites. J Neurosci. 2005 Dec 14;25(50):11531–41.
Deng, Qingwei, et al. “A C-terminal domain directs Kv3.3 channels to dendrites.J Neurosci, vol. 25, no. 50, Dec. 2005, pp. 11531–41. Pubmed, doi:10.1523/JNEUROSCI.3672-05.2005.
Deng Q, Rashid AJ, Fernandez FR, Turner RW, Maler L, Dunn RJ. A C-terminal domain directs Kv3.3 channels to dendrites. J Neurosci. 2005 Dec 14;25(50):11531–11541.

Published In

J Neurosci

DOI

EISSN

1529-2401

Publication Date

December 14, 2005

Volume

25

Issue

50

Start / End Page

11531 / 11541

Location

United States

Related Subject Headings

  • Shaw Potassium Channels
  • Rats
  • Protein Structure, Tertiary
  • Peptide Fragments
  • Neurons, Afferent
  • Neurology & Neurosurgery
  • Molecular Sequence Data
  • Mice
  • Gymnotiformes
  • Fish Proteins