Related Experiment Video
Updated: Nov 7, 2025
13:52
Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
Published on: March 19, 2014
23.6K
Emerging evidence for kindlin oligomerization and its role in regulating kindlin function
Wenting Bu1,2, Zarina Levitskaya1, Suet-Mien Tan1
1School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore637551.
Journal of Cell Science
|April 29, 2021
Summary
Kindlin proteins regulate integrin activation, crucial for cell-ECM interactions. Recent structural studies reveal how kindlin oligomerization impacts integrin binding and cell adhesion.
Area of Science:
- Biochemistry
- Cell Biology
- Structural Biology
Background:
- Integrin-ECM interactions are vital in physiological and pathological processes.
- Kindlins (FERMT1, FERMT2, FERMT3) are key positive regulators of integrin activation.
- Kindlin family members share structural similarities but have distinct functions.
Purpose of the Study:
- To review recent advancements in determining kindlin structures.
- To discuss the implications of kindlin structures for integrin activation.
- To explore the role of kindlin oligomerization in integrin binding and focal adhesion localization.
Main Methods:
- Analysis of recently obtained atomic structures of kindlins.
- Structural comparison of free kindlins and kindlin-β-integrin complexes.
- Review of emerging evidence on kindlin oligomerization.
Main Results:
- New structural data provides insights into kindlin function.
- Kindlin oligomerization emerges as a potential regulator of integrin binding.
- Oligomerization may influence kindlin localization at focal adhesions.
Conclusions:
- Structural biology has significantly advanced our understanding of kindlins.
- Kindlin oligomerization is a critical factor influencing integrin activation.
- Further research into kindlin oligomerization regulation is warranted.
Related Concept Videos
01:09Cytoskeletal Linker Proteins - Plakins
2.6K
Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
2.6K
01:15Activation of Integrins
4.3K
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...
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...
4.3K
01:39Mechanism of Filopodia Formation
2.7K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.7K
01:19Actin Filament Depolymerization
3.4K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
In F-actin, the ADF/cofilin proteins...
3.4K
01:17Intracellular Signaling Affects Focal Adhesions
3.1K
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...
Some...
3.1K
01:31Mechanism of Lamellipodia Formation
3.1K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
3.1K