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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.
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...
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.
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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...
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...

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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
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Published on: June 13, 2014

Structural requirements for activation in alphaIIb beta3 integrin.

Tetsuji Kamata1, Makoto Handa, Sonomi Ito

  • 1Department of Anatomy, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan. kamata@sc.itc.keio.ac.jp

The Journal of Biological Chemistry
|October 2, 2010
PubMed
Summary

Integrin activation involves a switchblade-like movement from bent to extended conformations. This study confirms bent integrins have low affinity and extended integrins have high affinity, dependent on specific structural changes.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Integrins mediate cell adhesion and signaling through conformational changes.
  • The switchblade model proposes integrin activation involves a transition from bent (low affinity) to extended (high affinity) states.
  • Conflicting reports exist regarding bent integrin ligand binding and extension-induced activation.

Purpose of the Study:

  • To investigate whether integrin affinity is regulated by a switchblade-like movement.
  • To engineer and analyze mutant integrins locked in bent or extended conformations.
  • To elucidate the structural requirements for extension-induced integrin activation.

Main Methods:

  • Engineering of mutant αIIbβ3 integrins constrained in bent or extended conformations using disulfide bridges and N-glycosylation sites.
  • Expression of mutant integrins in mammalian cells.
  • Assessment of fibrinogen binding to cells expressing engineered integrins.

Main Results:

  • Bent integrins failed to bind fibrinogen unless disulfide bridges were disrupted, indicating low affinity.
  • Extended integrins showed maximal activation with specific N-glycosylation site placement.
  • Extension-induced activation was dependent on the swing-out of the hybrid domain.

Conclusions:

  • Bent and extended integrin conformations correspond to low and high affinity states, respectively.
  • Integrin extension-induced activation relies on the swing-out of the hybrid domain.
  • Findings support the switchblade model for integrin affinity regulation.