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Related Concept Videos

Smooth Muscle Contraction01:25

Smooth Muscle Contraction

Smooth muscle contraction is a complex process vital for various bodily functions, from maintaining blood vessel tension to facilitating the movement of food through the digestive tract. Unlike striated muscles, smooth muscle contraction begins more slowly and lasts longer.
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

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...
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

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 characterized.
Structure and Organization of Smooth Muscles01:13

Structure and Organization of Smooth Muscles

Smooth muscle tissue is a type of muscle tissue that can be found lining various vital organs in the human body, including the lungs, blood vessels, digestive tract, and respiratory tract. This type of tissue is responsible for regulating the movements of these organs, playing crucial roles in the functioning of various systems, including the vascular, digestive, respiratory, and urinary systems.
Structure of smooth muscle cell
Smooth muscle cells are spindle-shaped with tapering ends and a...
Role of Myosin in Cell Migration01:18

Role of Myosin in Cell Migration

Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
Myosin II  is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction. It is...

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Related Experiment Video

Updated: Jul 17, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
08:57

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays

Published on: February 4, 2021

Vascular Smooth Muscle Myosin 2 Filaments Dynamically Assemble and Stabilize During Induced Contractility.

Sasha K Demeulenaere1, Margaret A Bennett1, Bradley Somerfield1

  • 1Department of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL.

Arteriosclerosis, Thrombosis, and Vascular Biology
|July 16, 2026
PubMed
Summary

Smooth muscle myosin II (SMII) dynamically assembles into filaments within vascular smooth muscle cells (SMCs). Induced contraction stabilizes these SMII filaments, allowing cells to adapt contractility and regulate blood pressure.

Keywords:
actinsblood pressuremuscle, smoothphosphorylationprotein kinases

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Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
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Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
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Last Updated: Jul 17, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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Published on: February 4, 2021

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Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
06:53

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Area of Science:

  • Cell Biology
  • Biophysics
  • Vascular Biology

Background:

  • Vascular smooth muscle cells (SMCs) regulate blood pressure and vessel integrity through dynamic changes in diameter.
  • Smooth muscle myosin II (SMII) is the primary motor protein responsible for SMC contraction, assembling into filaments that interact with actin.
  • The precise mechanisms of SMII filament assembly and dynamics in living SMCs, especially during contraction, are not fully understood.

Purpose of the Study:

  • To investigate the dynamic assembly and exchange kinetics of SMII filaments in vascular SMCs.
  • To characterize SMII dynamics at steady state and during induced contractility.
  • To explore the coassembly of SMII with other myosin isoforms and its role in force generation.

Main Methods:

  • Utilized single-cell filament assembly assays and fluorescence recovery after photobleaching (FRAP) in rat aortic SMCs expressing EGFP-tagged SMII.
  • Employed traction force microscopy to measure force production during SMII dynamics.
  • Developed a knock-in murine model for endogenous EGFP-SMII expression in primary SMCs and intact arterioles.

Main Results:

  • Induced contraction significantly increased SMII filament assembly and stabilized existing filaments.
  • FRAP revealed rapid SMII exchange kinetics, comparable to nonmuscle myosin II, not striated myosin II.
  • Super-resolution imaging indicated coassembly of SMII with nonmuscle myosin II filaments.
  • Studies in endogenous SMII models confirmed cell culture findings regarding dynamics and stabilization.

Conclusions:

  • SMII exhibits surprisingly dynamic behavior and coassembles with nonmuscle myosin II in vascular SMCs.
  • Vascular SMC activation enhances SMII filament assembly and stabilizes the dynamic SMII pool during force generation.
  • These dynamics allow vascular SMCs to adapt their contractility in response to physiological demands.