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

6.0K
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,...
6.0K
Activation of Integrins01:15

Activation of Integrins

5.5K
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...
5.5K
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

3.8K
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...
3.8K
Laminins are the Adhesive Proteins of Basal Lamina00:55

Laminins are the Adhesive Proteins of Basal Lamina

4.1K
Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
4.1K
Structure of Cadherins01:25

Structure of Cadherins

5.2K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
5.2K
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

4.5K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
4.5K

You might also read

Related Articles

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

Sort by
Same author

Cobalt-Catalyzed Hydrogen-Bond-Promoted Tandem Cyclization and Oxygen Migration: Access to Sterically Congested Fused Tetrahydro-β-Carbolines.

Organic letters·2026
Same author

Photoinduced Dearomative Oxyimination of Indoles Using Oxime Esters as Bifunctional Radical Precursors.

Organic letters·2026
Same author

Endoscopic retrograde appendicitis therapy: Progress in clinical application.

World journal of gastrointestinal endoscopy·2026
Same author

Hidden blood loss in anterior cervical discectomy and fusion versus single-level anterior cervical corpectomy and fusion with adjacent discectomy for two-level cervical spondylotic myelopathy.

Joint diseases and related surgery·2025
Same author

[A finite element biomechanical study of anterior transpedicular root screw plate fixation system in the lower cervical spine].

Zhongguo gu shang = China journal of orthopaedics and traumatology·2025
Same author

Mild and efficient construction of nitrogen-containing heterocycles from <i>ortho</i>-ethynylbenzaldehydes and anilines.

Organic & biomolecular chemistry·2025

Related Experiment Video

Updated: Mar 25, 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

8.1K

Three-Dimensional Structures of Full-Length, Membrane-Embedded Human α(IIb)β(3) Integrin Complexes.

Xiao-Ping Xu1, Eldar Kim1, Mark Swift1

  • 1Bioinformatics and Structural Biology Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California.

Biophysical Journal
|February 25, 2016
PubMed
Summary

Human integrin αIIbβ3 exists in four main conformations, shifting towards an upright state when activated by talin and ligands. This reveals new insights into integrin structure and activation mechanisms.

More Related Videos

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.7K
Imaging Protein-protein Interactions in vivo
11:15

Imaging Protein-protein Interactions in vivo

Published on: October 10, 2010

22.0K

Related Experiment Videos

Last Updated: Mar 25, 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

8.1K
Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.7K
Imaging Protein-protein Interactions in vivo
11:15

Imaging Protein-protein Interactions in vivo

Published on: October 10, 2010

22.0K

Area of Science:

  • Structural biology
  • Biochemistry
  • Cell biology

Background:

  • Integrins are crucial transmembrane receptors involved in hemostasis and arterial thrombosis.
  • Understanding integrin conformational dynamics is key to deciphering their function in health and disease.

Purpose of the Study:

  • To determine the three-dimensional structures of human integrin αIIbβ3 in near-physiological conditions.
  • To investigate the conformational equilibrium of integrin αIIbβ3 in the presence of cytosolic regulators and extracellular ligands.

Main Methods:

  • Cryo-electron microscopy
  • Multireference single-particle reconstruction
  • Computational fitting approaches
  • Lipid bilayer nanodiscs

Main Results:

  • Identified four main conformational states of integrin αIIbβ3, ranging from bent to fully upright.
  • Demonstrated a significant shift towards the upright conformation upon binding talin and ligands.
  • Revealed that ectodomain extension occurs without leg separation and the ligand-binding pocket remains accessible.

Conclusions:

  • Integrin activation involves shifts in conformational equilibrium, influenced by cytosolic and extracellular factors.
  • The study provides unprecedented 3D structural data of intact integrins under near-physiological conditions.
  • Findings suggest integrin activation mechanisms are linked to dynamic conformational changes within the membrane bilayer.