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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.
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,...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
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:...

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Related Experiment Video

Updated: Jul 1, 2026

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
13:52

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Published on: March 19, 2014

ILK binding to β1 integrin is indirect and mediated by kindlin-2.

Susanne C M Reinhardt1,2, Ralph T Böttcher3, Florian Brod3

  • 1Research Group Molecular Imaging and Bionanotechnology, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|June 29, 2026
PubMed
Summary

Kindlin-2 (K2) is essential for recruiting integrin-linked kinase (ILK) to focal adhesions, thereby regulating cell adhesion and signaling. This study clarifies the hierarchical relationship between K2 and ILK in focal adhesions.

Keywords:
focal adhesionsintegrin biologysuperresolution microscopy

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

Published on: June 13, 2014

Area of Science:

  • Cell biology
  • Biochemistry
  • Molecular biology

Background:

  • Integrin-linked kinase (ILK) and kindlin-2 (K2) are crucial for focal adhesion (FA) assembly, cell-matrix adhesion, and integrin signaling.
  • The precise mechanisms governing the interaction and localization of ILK and K2 within FAs, and their direct binding to integrins, are not fully understood.

Purpose of the Study:

  • To elucidate the hierarchical relationship between ILK and K2 in focal adhesions.
  • To determine the mechanism by which ILK and K2 interact with and regulate integrin function.
  • To establish a robust workflow for studying protein-protein interactions in cellular contexts.

Main Methods:

  • Utilized a combination of biochemistry, cell biology, and superresolution microscopy.
  • Developed a sensitive workflow to analyze protein-protein interactions and construct interaction networks.
  • Employed an analytical framework to differentiate direct from indirect molecular interactions.

Main Results:

  • Disruption of the ILK-K2 interaction led to reduced ILK localization in FAs and impaired integrin function.
  • Kindlin-2 (K2) recruitment to FAs remained unaffected when the ILK-K2 interaction was disrupted.
  • ILK does not directly bind to β1-integrin cytosolic domains; instead, K2 bridges ILK and β1 integrins for ILK recruitment.

Conclusions:

  • Kindlin-2 (K2) plays an essential role in recruiting integrin-linked kinase (ILK) to focal adhesions.
  • The K2-dependent recruitment of ILK is critical for proper integrin adhesion and signaling.
  • This study defines a clear hierarchical interaction between K2 and ILK in the regulation of focal adhesion dynamics and integrin function.