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

Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Introduction to Actin01:26

Introduction to Actin

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 different species.
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
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...
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.

You might also read

Related Articles

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

Sort by
Same author

A smartphone analogy to explore the origin of animals.

The EMBO journal·2026
Same author

Expression Atlas in 2026: enabling FAIR and open expression data through community collaboration and integration.

Nucleic acids research·2025
Same author

The mechanical response of vinculin.

Science advances·2025
Same author

Actin-driven nanotopography promotes stable integrin adhesion formation in developing tissue.

Nature communications·2024
Same author

Corrigendum to: A clinical, molecular genetics and pathological study of a FTDP-17 family with a heterozygous splicing variant c.823-10 G>T at the intron 9/exon 10 of the MAPT gene.

Neurobiology of aging·2024
Same author

A new experimental evidence-weighted signaling pathway resource in FlyBase.

Development (Cambridge, England)·2024

Related Experiment Video

Updated: Jul 18, 2026

Imaging Integrin Tension and Cellular Force at Submicron Resolution with an Integrative Tension Sensor
07:20

Imaging Integrin Tension and Cellular Force at Submicron Resolution with an Integrative Tension Sensor

Published on: April 25, 2019

Integrins and the actin cytoskeleton.

Isabelle Delon1, Nicholas H Brown

  • 1The Gurdon Institute and Dept of Physiology, Development and Neuroscience, University of Cambridge, Tennis Court Rd, Cambridge CB2 1QN.

Current Opinion in Cell Biology
|December 23, 2006
PubMed
Summary

Integrins link to the actin cytoskeleton via associated proteins, influencing cell adhesion. Genetic studies reveal how these protein complexes assemble and disassemble, controlling cellular movement and function.

More Related Videos

Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy
08:44

Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy

Published on: July 20, 2022

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin
08:37

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin

Published on: November 18, 2011

Related Experiment Videos

Last Updated: Jul 18, 2026

Imaging Integrin Tension and Cellular Force at Submicron Resolution with an Integrative Tension Sensor
07:20

Imaging Integrin Tension and Cellular Force at Submicron Resolution with an Integrative Tension Sensor

Published on: April 25, 2019

Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy
08:44

Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy

Published on: July 20, 2022

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin
08:37

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin

Published on: November 18, 2011

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Integrins are crucial cell surface receptors mediating cell adhesion.
  • The connection between integrins and the actin cytoskeleton is vital for cell adhesion and migration.
  • A complex of associated proteins links integrins to the cytoskeleton, regulating this interaction.

Purpose of the Study:

  • To elucidate the role of integrin-associated proteins in linking integrins to the actin cytoskeleton.
  • To understand how these protein complexes regulate the assembly and disassembly of the integrin-cytoskeleton linkage.
  • To explore the diverse signaling pathways from integrins to the cytoskeleton and their impact on cellular functions.

Main Methods:

  • Genetic analysis to determine the contribution of different protein components.
  • Biochemical assays to study protein complex assembly and disassembly.
  • Cellular imaging to visualize integrin-cytoskeleton interactions and cellular structures.

Main Results:

  • Identified key integrin-associated proteins involved in cytoskeleton linkage.
  • Demonstrated that integrin-cytoskeleton connections can be dynamically regulated.
  • Showcased context-dependent roles of integrins in stimulating or suppressing actin structures.
  • Highlighted the reciprocal influence of the cytoskeleton on integrin junction strength and stability.

Conclusions:

  • Integrin-mediated adhesion is tightly regulated by associated protein complexes and the actin cytoskeleton.
  • Dynamic remodeling of the integrin-cytoskeleton link is essential for cell movement and function.
  • Understanding these interactions provides insights into cellular mechanics and signaling pathways.