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Related Concept Videos

The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

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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...
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Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Types of Intermediate Filaments01:31

Types of Intermediate Filaments

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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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Disassembly of Intermediate Filaments01:35

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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Adaptability of Cytoskeletal Filaments01:12

Adaptability of Cytoskeletal Filaments

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The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
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Deimination, Intermediate Filaments and Associated Proteins.

Julie Briot1, Michel Simon1, Marie-Claire Méchin1

  • 1UDEAR, Institut National de la Santé Et de la Recherche Médicale, Université Toulouse III Paul Sabatier, Université Fédérale de Toulouse Midi-Pyrénées, U1056, 31059 Toulouse, France.

International Journal of Molecular Sciences
|November 24, 2020
PubMed
Summary

Deimination, a modification by peptidylarginine deiminases (PADs), impacts intermediate filament proteins and associated proteins. This study explores deimination

Keywords:
citrullinationcytoskeletonfilaggrinkeratinpeptidylarginine deiminasepost-translational modification

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Deimination (citrullination) is a calcium-dependent post-translational modification catalyzed by peptidylarginine deiminases (PADs).
  • This modification plays roles in physiological processes and is implicated in autoimmune diseases, cancers, and neurodegenerative disorders.
  • Intermediate filaments (IF) and associated proteins (IFAP) are key substrates of PAD enzymes.

Purpose of the Study:

  • To investigate the effects of deimination on the polymerization and solubility of intermediate filament proteins.
  • To examine the impact of deimination on the proteolysis and cross-linking of intermediate filament-associated proteins.
  • To highlight the features and limitations of citrullinomes in the context of deimination.

Main Methods:

  • Analysis of protein polymerization and solubility changes upon deimination.
  • Assessment of proteolysis and cross-linking of IFAP following deimination.
  • Characterization of citrullinomes to identify deimination-specific modifications.

Main Results:

  • Deimination significantly alters the polymerization and solubility characteristics of IF proteins.
  • PAD-mediated deimination affects the susceptibility of IFAP to proteolysis and influences their cross-linking patterns.
  • Citrullinome analysis reveals specific deimination sites and their functional consequences.

Conclusions:

  • Deimination is a critical regulator of IF and IFAP properties with implications for cellular functions and disease pathogenesis.
  • Understanding deimination's effects on these proteins is crucial for deciphering their roles in health and disease.
  • Citrullinome studies offer valuable insights but require careful consideration of their limitations.