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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

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.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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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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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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Related Experiment Video

Updated: Nov 4, 2025

Imaging Intermediate Filaments and Microtubules with 2-dimensional Direct Stochastic Optical Reconstruction Microscopy
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Imaging Intermediate Filaments and Microtubules with 2-dimensional Direct Stochastic Optical Reconstruction Microscopy

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Intermediate filaments.

Gaëlle Dutour-Provenzano1, Sandrine Etienne-Manneville2

  • 1Cell Polarity, Migration and Cancer Unit, Institut Pasteur, UMR3691 CNRS, Équipe Labellisée Ligue Contre le Cancer, F-75015 Paris, France; Sorbonne Université, Collège Doctoral, F-75005 Paris, France.

Current Biology : CB
|May 25, 2021
PubMed
Summary

Intermediate filaments are a type of cytoskeletal structure found in animal cells. Unlike actin and microtubules, they do not rely on nucleotides to assemble and lack intrinsic polarity. These properties allow them to form stable, adaptable networks. Recent studies show IFs are crucial for cell and tissue integrity. Mutations in IF genes are linked to various diseases. This Primer reviews evidence that IFs are a unique and essential part of the cytoskeleton, contributing to both cytoplasmic and nuclear functions. Their structure and behavior set them apart from other filaments, making them a key focus in cell biology.

Keywords:
cytoskeletoncell biologytissue integrityintermediate filaments

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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
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Area of Science:

  • Cell biology
  • Cytoskeletal research
  • Intermediate filaments in tissue integrity

Background:

Cytoskeletal networks govern cell shape and mechanics. Actin and microtubules are well-studied, but IFs remain less understood. Prior research has shown IFs differ structurally and functionally from other filaments. Their 10 nm diameter was once a defining trait, but recent findings challenge this view. IFs lack intrinsic polarity and nucleotide dependence, making them distinct. No prior work had resolved their full functional scope. This gap motivated renewed investigation into IF roles. Their role in disease and cell integrity now drives increased study.

Purpose Of The Study:

This Primer aims to clarify the unique properties of IFs. It addresses how IFs differ from actin and microtubules. The study focuses on IF structure and function in cell architecture. It explores their role in tissue integrity and disease. IFs are not intermediate in behavior, despite their name. The authors seek to highlight recent discoveries about IF dynamics. They emphasize IFs as tunable, cell-type-specific networks. Their goal is to explain why IFs are now central to cytoskeletal research.

Main Methods:

The authors review recent literature on IF structure and function. They analyze IF assembly mechanisms and mechanical properties. No experimental data is presented, as this is a literature review. The focus is on synthesizing findings from multiple studies. IFs are compared to actin and microtubules in structure and behavior. The review includes evidence from disease-linked IF mutations. It integrates findings on IF roles in cytoplasmic and nuclear functions. The authors summarize key discoveries from the last decade.

Main Results:

IFs are structurally distinct from actin and microtubules. They assemble without nucleotide dependence, unlike other filaments. IFs form stable, cell-type-specific networks. Their role in cell and tissue integrity is now well-documented. Mutations in IF genes are linked to numerous human diseases. IFs contribute to nuclear and cytoplasmic functions. They provide tunable mechanical support to cells. These findings suggest IFs are essential for cellular resilience.

Conclusions:

IFs are not intermediate in function or behavior. Their unique properties set them apart from other cytoskeletal elements. The authors synthesize evidence of IF roles in cell integrity. IFs are now recognized for their stability and adaptability. Their lack of polarity and nucleotide dependence is key to their function. The review highlights IFs as a tunable component of the cytoskeleton. IFs contribute to both cytoplasmic and nuclear processes. These conclusions are based on recent studies and disease associations.

Intermediate filaments lack intrinsic polarity and nucleotide dependence, making them structurally and functionally unique.

Numerous human diseases are linked to IF gene mutations, though specific examples are not detailed in the abstract.

The lack of polarity allows IFs to form stable, non-directional networks, contributing to their mechanical resilience.

Tunable networks allow IFs to adapt to cell-type-specific needs, supporting both cytoplasmic and nuclear functions.

IFs provide mechanical stability and resilience, which are essential for maintaining tissue structure under stress.

The authors propose that IFs are a key cytoskeletal element with unique structural and functional properties.