Physiological and Pathophysiological Insights of Nav1.4 and Nav1.5 Comparison.

Mutations in Nav1.4 and Nav1.5 α-subunits have been associated with muscular and cardiac channelopathies, respectively.

Dynamitin affects cell-surface expression of voltage-gated sodium channel Nav1.5.

The major cardiac voltage-gated sodium channel Nav1.5 associates with proteins that regulate its biosynthesis, localization, activity and degradation. Identification of partner proteins is crucial for a better understanding of the channel regulation.

IKs response to protein kinase A-dependent KCNQ1 phosphorylation requires direct interaction with microtubules.

Aims: KCNQ1 (alias KvLQT1 or Kv7.1) and KCNE1 (alias IsK or minK) co-assemble to form the voltage-activated K(+) channel responsible for I(Ks)-a major repolarizing current in the human heart-and their dysfunction promotes cardiac arrhythmias. The channel is a component of larger macromolecular complexes containing known and undefined regulatory proteins.

Mutations in the gene encoding filamin A as a cause for familial cardiac valvular dystrophy.

Background: Myxomatous dystrophy of the cardiac valves affects approximately 3% of the population and remains one of the most common indications for valvular surgery. Familial inheritance has been demonstrated with autosomal and X-linked transmission, but no specific molecular abnormalities have been documented in isolated nonsyndromic forms. We have investigated the genetic causes of X-linked myxomatous valvular dystrophy (XMVD) previously mapped to chromosome Xq28.

14-3-3 is a regulator of the cardiac voltage-gated sodium channel Nav1.5.

The voltage-sensitive Na(+) channel Na(v)1.5 plays a crucial role in generating and propagating the cardiac action potential and its dysfunction promotes cardiac arrhythmias. The channel takes part into a large molecular complex containing regulatory proteins.