Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

6.4K
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...
6.4K
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

26.6K
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...
26.6K
Role of Myosin in Cell Migration01:18

Role of Myosin in Cell Migration

2.8K
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....
2.8K
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

4.7K
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...
4.7K
Introduction to Actin01:26

Introduction to Actin

4.6K
Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
4.6K
The Sarcomere01:08

The Sarcomere

18.2K
A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each...
18.2K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Proteomic profiling reveals structural and adhesion pathways regulated by the inverted CHRFAM7AΔ2bp variant in human neural progenitor cells.

BMC neuroscience·2026
Same author

Binary partitioning of human brain organization due to divergent human cytoskeletal evolution.

bioRxiv : the preprint server for biology·2026
Same author

FURIN Stimulates NOTCH2 and NOTCH3 Pathways, Leading to Return of Function in Aged Cells.

Life (Basel, Switzerland)·2026
Same author

Developing Topics.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025
Same author

Developing Topics.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025
Same author

Developing Topics.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025

Related Experiment Video

Updated: May 2, 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

5.3K

Tissue specific expression of myosin IC isoforms.

Neil L Sielski, Ivanna Ihnatovych, Jacob J Hagen

  • 1Department of Physiology and Biophysics, University at Buffalo-State University of New York, 3435 Main Street, Buffalo, NY 14214, USA. whofmann@buffalo.edu.

BMC Cell Biology
|March 13, 2014
PubMed
Summary
This summary is machine-generated.

Myosin IC isoforms A and B exhibit distinct expression patterns in mouse tissues. Myosin IC isoform A shows tissue-specific expression, while isoform B is ubiquitously expressed, suggesting unique functional roles.

More Related Videos

Author Spotlight: Isolation of Long Muscle Fibers from Mouse Hindlimb Muscles for Studying Excitation-Contraction Coupling Across Fiber Types
08:12

Author Spotlight: Isolation of Long Muscle Fibers from Mouse Hindlimb Muscles for Studying Excitation-Contraction Coupling Across Fiber Types

Published on: December 1, 2023

3.6K
A Rapid Automated Protocol for Muscle Fiber Population Analysis in Rat Muscle Cross Sections Using Myosin Heavy Chain Immunohistochemistry
05:57

A Rapid Automated Protocol for Muscle Fiber Population Analysis in Rat Muscle Cross Sections Using Myosin Heavy Chain Immunohistochemistry

Published on: March 28, 2017

10.5K

Related Experiment Videos

Last Updated: May 2, 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

5.3K
Author Spotlight: Isolation of Long Muscle Fibers from Mouse Hindlimb Muscles for Studying Excitation-Contraction Coupling Across Fiber Types
08:12

Author Spotlight: Isolation of Long Muscle Fibers from Mouse Hindlimb Muscles for Studying Excitation-Contraction Coupling Across Fiber Types

Published on: December 1, 2023

3.6K
A Rapid Automated Protocol for Muscle Fiber Population Analysis in Rat Muscle Cross Sections Using Myosin Heavy Chain Immunohistochemistry
05:57

A Rapid Automated Protocol for Muscle Fiber Population Analysis in Rat Muscle Cross Sections Using Myosin Heavy Chain Immunohistochemistry

Published on: March 28, 2017

10.5K

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • Myosin IC, a single-headed myosin, functions in both cytoplasmic and nuclear processes.
  • Mammalian cells express three myosin IC isoforms (A, B, C) differing in N-terminal peptides.
  • Expression patterns and regulatory mechanisms of myosin IC isoforms are largely unknown.

Purpose of the Study:

  • To investigate the expression patterns of myosin IC isoforms A and B.
  • To elucidate tissue-specific regulation of the MYOIC gene.

Main Methods:

  • Comprehensive expression analysis of myosin IC isoforms A and B.
  • Immunoblotting using isoform-specific antibodies.
  • Quantitative reverse transcription PCR (qRT-PCR) with isoform-specific primers.

Main Results:

  • Myosin IC isoforms A and B display distinct tissue expression profiles in mice.
  • Myosin IC isoform A exhibits tissue-specific expression.
  • Myosin IC isoform B is ubiquitously expressed at consistent levels across tissues.

Conclusions:

  • Distinct expression profiles suggest tissue-specific regulation of the MYOIC gene.
  • Myosin IC isoforms likely possess unique, tissue-specific functions despite sequence homology.