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,...
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.
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...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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...
Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

You might also read

Related Articles

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

Sort by
Same author

mRNA delivery of a class 1/4 SARS-CoV-2 neutralizing antibody protects against diverse sarbecoviruses in a lethal mouse challenge model.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Plastics in the Perioperative Period: Deleterious Health Effects on Patients and Providers.

Anesthesiology·2026
Same author

Enzymatic Biocontrol of Fire Blight (<i>Erwinia amylovora</i>) Using an Engineered Glycosyl Hydrolase.

Environmental science & technology·2026
Same author

Deep mining of the human antibody repertoire identifies frequent and genetically diverse CDRH3 topologies targetable by vaccination.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Enzyme-enhanced RNA isolation from biofilm-producing bacteria.

Microbiology spectrum·2026
Same author

Immune-focused RBD nanoparticles induce cross-reactive, RBS-directed responses capable of variant-resistant SARS-CoV-2 neutralization.

PLoS pathogens·2026

Related Experiment Video

Updated: Jun 17, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Consensus motif for integrin transmembrane helix association.

Bryan W Berger1, Daniel W Kulp, Lisa M Span

  • 1Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 19, 2010
PubMed
Summary
This summary is machine-generated.

Integrin transmembrane helices interact via a conserved "reciprocating large-small motif." Disrupting this motif activates integrins, revealing its role as a crucial on-off switch in cellular adhesion.

More Related Videos

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Related Experiment Videos

Last Updated: Jun 17, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Transmembrane (TM) helix interactions regulate biological functions, including integrin activity.
  • Integrin TM helix interactions are crucial for cellular adhesion but difficult to characterize.
  • Disruption of resting-state integrin TM helix interactions leads to activation.

Purpose of the Study:

  • To define the sequence motif governing TM helix interactions in beta (1) and beta (3) integrin subfamilies.
  • To investigate the role of TM helix associations in integrin activation.
  • To characterize the specificity and affinity of integrin TM helix interactions.

Main Methods:

  • Development of a bacterial reporter system to study TM helix associations.
  • Analysis of sequence motifs required for helix-helix interactions.
  • Site-directed mutagenesis to destabilize the identified motif in full-length integrins.

Main Results:

  • Identified a novel three-dimensional motif, the "reciprocating large-small motif," for TM helix interactions.
  • Demonstrated that complementary packing of small and large groups stabilizes helix associations.
  • Showed that mutations destabilizing this motif activate native integrins.

Conclusions:

  • The conserved "reciprocating large-small motif" is a vital, widespread on-off switch for integrin activation.
  • This motif integrates with other control elements to regulate integrin function.
  • Specific stabilization of TM helix associations is achieved through this conserved motif.