English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Sodium channels play pivotal roles in health and diseases due to their ability to control cellular excitability. The pore-forming α-subunit (Naα) of the voltage-sensitive channels (i.e., Nav1.1-1.9) and the non-voltage-dependent channel (i.e., Nax) share a common structural motif and selectivity for sodium ions. We hypothesized that the actin based non-muscle myosin II motor proteins (NM-IIs), non-muscle myosin heavy chain (NMHC)-IIA/myh9 and NMHC-IIB/myh10, might interact with Naα subunits to play an important role in their transport, trafficking and/or function. Immunochemical and electrophysiological assays were conducted using rodent nervous (brain and dorsal root ganglia (DRG)) tissues and ND7/23 cells co-expressing Nav subunits and recombinant myosins. Immunoprecipitation of myh9 and myh10 from rodent brain tissues led to the co-immunoprecipitation of Nax, Nav1.2 and Nav1.3 subunits, but not Nav1.1 and Nav1.6 subunits, expressed there. Similarly, immunoprecipitation of myh9 and myh10 from rodent DRG tissues led to the co-immunoprecipitation of Nav1.7 and Nav1.8 subunits, but not Nav1.9 subunits, expressed there. The functional implication of one of these interactions were assessed by co-expressing myh10 along with Nav1.8 subunits in ND7/23 cells. Myh10 overexpression led to 3-fold increase (p<0.01) in the current density of Nav1.8 channels expressed in ND7/23 cells. Myh10 co-expression also hyperpolarized voltage-dependent activation and steady-state fast-inactivation of Nav1.8 channels. Additionally, co-expression of myh10 reduced (P < 0.01) the offset of fast-inactivation and the amplitude of the ramp currents of Nav1.8 channels. These results indicate that NMHC-IIs interact with Naα subunits in an isoform-dependent manner and influence their functional properties.

Nonmuscle myosin II isoforms interact with sodium channel alpha subunits