Abstract
The voltage-gated sodium channel is vital for cardiomyocyte function, and consists of a protein complex containing a pore-forming α subunit and two associated β subunits. A fundamental, yet unsolved, question is to define the precise function of β subunits. While their location in vivo remains unclear, large evidence shows that they regulate localization of α and the biophysical properties of the channel. The current data support that one of these subunits, β2, promotes cell surface expression of α. The main α isoform in an adult heart is NaV1.5, and mutations in SCN5A, the gene encoding NaV1.5, often lead to hereditary arrhythmias and sudden death. The association of β2 with cardiac arrhythmias has also been described, which could be due to alterations in trafficking, anchoring, and localization of NaV1.5 at the cardiomyocyte surface. Here, we will discuss research dealing with mechanisms that regulate β2 trafficking, and how β2 could be pivotal for the correct localization of NaV1.5, which influences cellular excitability and electrical coupling of the heart. Moreover, β2 may have yet to be discovered roles on cell adhesion and signaling, implying that diverse defects leading to human disease may arise due to β2 mutations.
Highlights
We often wonder why people get sick
It is estimated that around 6 million people die each year worldwide of Sudden Cardiac Death (SCD) due to ventricular arrhythmia, which is often associated with cardiomyopathy
It is known that several proteins interact with NaV1.5, including cytoskeleton been reported the assembly of macromolecular complexes between NaV 1.5 and the inward rectifier components, and various structural domains involved in these interactions have been identified potassium channel Kir2.1
Summary
We often wonder why people get sick. Why do some people die early in life while others reach old age without major health problems? It is obvious that both genetic and environmental factors are playing a role. To understand the role of the NaV channel in cardiac function, and the consequent alterations that contribution of its associated and regulatory proteins. It is known that several proteins interact with NaV1.5, including cytoskeleton been reported the assembly of macromolecular complexes between NaV 1.5 and the inward rectifier components, and various structural domains involved in these interactions have been identified potassium channel Kir2.1 It has been reported the assembly of macromolecular complexes between resting membrane potential of ventricular cardiomyocytes), which localize together in microdomains. Understanding how all these molecules interact to regulate the subcellular localization of NaV channels is clearly a challenge in this field of research
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