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Related Concept Videos

Types of Intermediate Filaments01:31

Types of Intermediate Filaments

The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
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The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...
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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.
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Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
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Integrin binding immunoglobulin type filamin domains have variable stability.

Pengju Jiang1, Iain D Campbell

  • 1Biochemistry Department, University of Oxford, Oxford, UK.

Biochemistry
|September 27, 2008
PubMed
Summary
This summary is machine-generated.

Filamin Ig-like domains, particularly FLNa21, show surprising instability, even under physiological conditions. However, integrin binding significantly enhances FLNa21 stability, suggesting a role in mechanical force sensitivity.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Cellular Mechanics

Background:

  • Filamin is a large actin-binding protein crucial for cellular structure and force transmission.
  • Filamin comprises numerous immunoglobulin-like (Ig-like) domains, with specific modules mediating interactions with integrin receptors.
  • The mechanical properties and stability of these Ig-like domains are critical for filamin function.

Purpose of the Study:

  • To investigate the stability of filamin's Ig-like domains, focusing on module 21 (FLNa21), under varying pH and temperature conditions.
  • To determine how integrin binding affects the stability of FLNa21.
  • To compare the stability of FLNa21 with neighboring filamin Ig-like modules.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to study protein stability.
  • Experiments were conducted across a range of pH and temperatures to assess domain stability.
  • The binding of FLNa21 to integrin cytoplasmic tails was analyzed in conjunction with stability measurements.

Main Results:

  • FLNa21 exhibits partial unfolding even under physiological conditions and when associated with FLNa20.
  • FLNa21 is significantly less stable than homologous modules like FLNa19 and FLNa17.
  • Integrin binding markedly enhances the stability of FLNa21.

Conclusions:

  • The inherent instability of FLNa21 may contribute to filamin's sensitivity to cellular mechanical forces.
  • Integrin engagement stabilizes FLNa21, potentially modulating filamin's mechanical response.
  • Variability in Ig-like module stability is a key feature of filamin structure-function relationships.