September 10, 2003Journal of NeuroscienceOpen Access

Calmodulin Binds to the C Terminus of Sodium Channels Nav1.4 and Nav1.6 and Differentially Modulates Their Functional Properties

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Population

In vitro models expressing GST-fusion proteins containing C-terminal domains of Nav1.1-Nav1.9 and mutant…

Comparison

Disruption of interaction between calmodulin and… vs Wild-type or baseline conditions

Design

Preclinical

Authors

RHRaimund I. HerzogYale University LCLiu CQingdao University SWStephen G. WaxmanBoston University

Discussion

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Implication

Implicates CaM in NaV1.4/1.6 function; hypothesis-generating for channelopathy therapies, pending human validation.

Structured PICO

Population

In vitro models expressing GST-fusion proteins containing C-terminal domains of Nav1.1-Nav1.9 and mutant constructs of Nav1.4 and Nav1.6

Intervention

Disruption of interaction between calmodulin (CaM) and the C terminus of NaV1.4 and NaV1.6, and overexpression of CaM

Comparator

Wild-type or baseline conditions

Outcome

Current amplitude and densitysurrogate

Calmodulin regulates the functional expression and properties of voltage-gated sodium channels NaV1.4 and NaV1.6 via both calcium-dependent and calcium-independent mechanisms.

Cite This Study

Herzog et al. (2003) studied this question.

synapsesocial.com/papers/6a81650aec86ba91653c08aa https://doi.org/10.1523/jneurosci.23-23-08261.2003

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Calmodulin Binds to the C Terminus of Sodium Channels Nav1.4 and Nav1.6 and Differentially Modulates Their Functional Properties

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Calmodulin Binds to the C Terminus of Sodium Channels Nav1.4 and Nav1.6 and Differentially Modulates Their Functional Properties

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider