Related Experiment Video
Updated: Feb 8, 2026
09:55
Examining Monosynaptic Connections in Drosophila Using Tetrodotoxin Resistant Sodium Channels
Published on: February 14, 2018
10.3K
Nonmuscle myosin II isoforms interact with sodium channel alpha subunits
Bhagirathi Dash1,2,3, Chongyang Han1,2,3, Stephen G Waxman1,2,3
11 Department of Neurology, Yale University School of Medicine, New Haven, CT, USA.
Molecular Pain
|June 30, 2018
Summary
Nonmuscle myosin heavy chain-IIs (myh9 and myh10) interact with specific sodium channel alpha subunits, influencing their transport and function. This interaction impacts cellular excitability, with myh10 significantly altering Nav1.8 channel properties.
Area of Science:
- Neuroscience
- Cell Biology
- Molecular Biology
Background:
- Sodium channels (Nav subunits) are crucial for cellular excitability in health and disease.
- Nonmuscle myosin II motor proteins (myh9 and myh10) are actin-based motors involved in cellular processes.
Purpose of the Study:
- To investigate the potential interaction between nonmuscle myosin II motor proteins and sodium channel alpha subunits.
- To determine if these interactions influence sodium channel transport, trafficking, and/or function.
Main Methods:
- Immunochemical assays, including immunoprecipitation, were performed on rodent nervous tissues and ND7/23 cells.
- Electrophysiological assays were used to assess the functional impact of myosin-channel interactions.
- Coexpression of Nav subunits and recombinant myosins in ND7/23 cells.
Main Results:
- Immunoprecipitation revealed interactions between myh9/myh10 and specific Nav subunits (Nav subtypes: Nax, Nav1.2, Nav1.3, Nav1.7, Nav1.8) in a tissue-dependent manner.
- Coexpression of myh10 with Nav1.8 channels in ND7/23 cells significantly increased current density (three-fold).
- Myh10 coexpression altered Nav1.8 channel gating, including hyperpolarizing activation and inactivation, and reduced fast inactivation offset and ramp current amplitude.
Conclusions:
- Nonmuscle myosin heavy chain-IIs interact with sodium channel alpha subunits in an isoform-dependent manner.
- These interactions play a significant role in modulating the functional properties of sodium channels, impacting cellular excitability.
Related Concept Videos
01:08Antiepileptic Drugs: Sodium Channel Blockers
1.8K
Antiepileptic drugs are specialized medications that prevent seizures in individuals diagnosed with epilepsy. These drugs primarily function by blocking the movement of sodium ions through channels in the neuronal membrane, inhibiting the repetitive firing of action potentials often associated with seizures.
Sodium channel blockers modulate ion channels, particularly voltage-gated sodium channels. They block only sodium ion movement.
Among the most commonly prescribed antiepileptic drugs are...
Sodium channel blockers modulate ion channels, particularly voltage-gated sodium channels. They block only sodium ion movement.
Among the most commonly prescribed antiepileptic drugs are...
1.8K
01:22Antiarrhythmic Drugs: Class I Agents as Sodium Channel Blockers
3.3K
Class I antiarrhythmic drugs are used to treat various types of arrhythmias or irregular heart rhythms. These drugs block the sodium (Na+) channels in the cardiac cells, thereby affecting the movement of electrical impulses across the heart. Class I antiarrhythmic drugs are divided into three subgroups: Class IA, Class IB, and Class IC, each with distinct mechanisms of action and effects on the heart.
Class 1A Antiarrhythmic Drugs: These drugs work by moderately blocking sodium channels,...
Class 1A Antiarrhythmic Drugs: These drugs work by moderately blocking sodium channels,...
3.3K
01:16Actin and Myosin in Muscle Contraction
24.0K
Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
24.0K
01:19Ion Channels
91.5K
The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow...
Ion channels are specialized integral membrane proteins on the plasma membrane that allow...
91.5K
01:26Regulation of Sodium and Potassium
2.3K
The regulation of sodium and potassium ion concentrations in the human body is a complex process governed primarily by hormones such as aldosterone, antidiuretic hormone (ADH), and atrial natriuretic peptide (ANP).
Sodium Regulation
Sodium ions make up approximately 90% of extracellular cations, with a normal blood plasma concentration of 136–148 mEq/L. A decrease in blood volume and pressure triggers the release of renin from granular cells in the juxtaglomerular complex (JGC), primarily...
Sodium Regulation
Sodium ions make up approximately 90% of extracellular cations, with a normal blood plasma concentration of 136–148 mEq/L. A decrease in blood volume and pressure triggers the release of renin from granular cells in the juxtaglomerular complex (JGC), primarily...
2.3K
01:15Overview of Myosin Structure and Function
6.7K
Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X) have been well...
6.7K