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

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...
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,...
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:...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...

You might also read

Related Articles

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

Sort by
Same author

The β<sub>8</sub> integrin EGF domains support a constitutive extended conformation, and the cytoplasmic domain impairs outside-in signaling.

Journal of cellular physiology·2022
Same author

Effects of the association of the α<sub>v</sub> β<sub>8</sub> lower legs on integrin ligand binding.

Journal of cellular biochemistry·2021
Same author

Atypical structure and function of integrin α<sub>V</sub> β<sub>8</sub>.

Journal of cellular physiology·2020
Same author

The interface between the EGF1 and EGF2 domains is critical in integrin affinity regulation.

Journal of cellular biochemistry·2018
Same author

Structural basis of antifreeze activity of a bacterial multi-domain antifreeze protein.

PloS one·2017
Same author

Recrystallization inhibition in ice due to ice binding protein activity detected by nuclear magnetic resonance.

Biotechnology reports (Amsterdam, Netherlands)·2017
Same journal

Zinc Finger Proteins as Regulators of Organ Fibrosis.

Journal of cellular biochemistry·2026
Same journal

Intrinsic Disorder Status in Human Proteins Interacting With SARS-CoV-2 Proteins: Insights From Five Years of Translational Research.

Journal of cellular biochemistry·2026
Same journal

The Effect of Protein Tagging on Aggregation and Phase Separation.

Journal of cellular biochemistry·2026
Same journal

TRIM32 Alleviates the Inflammation in Spinal Cord Injury Progression Through Inducing the Ubiquitination Degradation of TLR4.

Journal of cellular biochemistry·2026
Same journal

Bedaquiline Binding at the Leading Site of Mycobacterium tuberculosis ATP Synthase Induces Distinct Structural and Dynamic Changes.

Journal of cellular biochemistry·2026
Same journal

Agrin Ablation in Osteoblasts Compromises Long Bone Structure and Osteoblastic Differentiation of Mesenchymal Stem Cells.

Journal of cellular biochemistry·2026
See all related articles

Related Experiment Video

Updated: Jun 18, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Structural basis of integrin transmembrane activation.

Wei Wang1, Bing-Hao Luo

  • 1Department of Biological Sciences, Louisiana State University, 202 Life Sciences Building, Baton Rouge, Louisiana 70803, USA.

Journal of Cellular Biochemistry
|December 2, 2009
PubMed
Summary
This summary is machine-generated.

Integrin activation involves conformational changes in transmembrane and cytoplasmic domains. A new model explains how these changes facilitate signaling across the cell membrane.

More Related Videos

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

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

Related Experiment Videos

Last Updated: Jun 18, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

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

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

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Signaling

Background:

  • Integrins are critical cell adhesion receptors mediating bidirectional transmembrane signaling.
  • Understanding integrin activation mechanisms requires detailed structural insights into their domains.
  • Conformational changes in integrin transmembrane (TM) and cytoplasmic domains are key to activation.

Purpose of the Study:

  • To elucidate the structural basis of integrin resting state and activation.
  • To propose a new model for integrin transmembrane activation.
  • To investigate the role of specific motifs in integrin alpha/beta subunit association.

Main Methods:

  • Rosetta computational modeling integrated with experimental data from intact mammalian cell surface integrins.
  • Analysis of structural differences between resting state integrins and monomeric alpha(IIb)beta(3) (active conformations) via NMR structures.
  • Comparative structural analysis of TM and cytoplasmic domains.

Main Results:

  • A resting state structure revealed ridge-in-groove packing of alpha(IIb) GXXXG and beta(3) TM motifs.
  • Specific motifs (alpha(IIb) GFFKR, beta(3) Lys-716) are critical for alpha/beta association in cytoplasmic segments.
  • Beta subunit helix tilting and lipid bilayer embedding occur during activation, distinct from the alpha subunit helix.

Conclusions:

  • A new model for integrin TM activation is proposed, with the recent NMR structure representing an intermediate state.
  • Electrostatic interactions in the cytoplasmic region are important for initiating alpha/beta association.
  • Conformational dynamics of TM and cytoplasmic domains are essential for integrin activation and signaling.