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Related Concept Videos

Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

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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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The Structure of Intermediate Filaments01:19

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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.
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Formation of Intermediate Filaments00:57

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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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Formation of Higher-order Actin Filaments01:11

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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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Assembly of Cytoskeletal Filaments01:18

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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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Assembly of Complex Microtubule Structures01:32

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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Updated: Nov 17, 2025

Imaging Intermediate Filaments and Microtubules with 2-dimensional Direct Stochastic Optical Reconstruction Microscopy
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Transiently structured head domains control intermediate filament assembly.

Xiaoming Zhou1, Yi Lin1, Masato Kato1,2,3

  • 1Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390.

Proceedings of the National Academy of Sciences of the United States of America
|February 17, 2021
PubMed
Summary
This summary is machine-generated.

The head domains of neurofilament light (NFL) and desmin intermediate filaments (IFs) can switch between disordered and ordered states. This structural flexibility influences their assembly and impacts cell shape.

Keywords:
in situ structural analysisintermediate filamentslabile cross-β structureslow complexity domainsphase separation

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Intermediate filaments (IFs), including neurofilament light (NFL) and desmin, are crucial for cell structure.
  • Low complexity (LC) head domains are essential for IF assembly.
  • The structural dynamics of these LC head domains are not fully understood.

Purpose of the Study:

  • To investigate the structural properties of isolated and assembled NFL and desmin head domains.
  • To explore the role of head domain self-interactions in IF assembly.
  • To understand how phosphorylation and mutations affect head domain behavior and IF formation.

Main Methods:

  • Solid-state Nuclear Magnetic Resonance (ss-NMR) spectroscopy.
  • Intein chemistry and segmental isotope labeling for protein preparation.
  • Analysis of head domain polymers and fully assembled IFs.

Main Results:

  • Isolated NFL and desmin head domains exist in disordered and labile, β-strand-enriched polymer states.
  • ss-NMR studies reveal structural order in these head domain polymers.
  • Assembled NFL and desmin IFs exhibit ss-NMR spectra similar to the β-strand-enriched polymers.
  • Phosphorylation and disease mutations alter self-association but impede IF assembly.

Conclusions:

  • The head domains of NFL and desmin IFs exhibit facultative structural assembly through labile, β-strand-enriched self-interactions.
  • This structural plasticity of head domains is critical for IF assembly and influences overall cell morphology.
  • Understanding these dynamics provides insights into intermediate filament-related diseases.