Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Disassembly of Intermediate Filaments

Disassembly of Intermediate Filaments

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Temporal analysis of pikeperch (Sander lucioperca) under heat stress: an integrated study from histological, physiological and transcriptomic perspectives.

Journal of thermal biology·2026

Same author

Association between 3 D CT-based volumetric fat infiltration of lumbar paraspinal muscles and bone mineral density: a clinical study.

BMC medical imaging·2026

Same author

A Kazal-type serine protease inhibitor PaSpink1 from silver pomfret (Pampus argenteus): antibacterial activity and protection against Vibrio parahaemolyticus-induced hepatocyte apoptosis.

International journal of biological macromolecules·2026

Same author

Enhanced Neural Responses to Self-Name Stimuli Relative to Tone and Reversed Speech Deviants in the Auditory Oddball Paradigm.

Brain sciences·2026

Same author

Identification and Transcriptome Resource of the Mite <i>Orthogalumna</i> cf. <i>terebrantis</i> (Acari: Galumnidae) in China.

Current issues in molecular biology·2026

Same author

Genome-wide identification of the cystatin gene family and functional characterization of cystatin B in flathead mullet (Mugil cephalus).

Fish & shellfish immunology·2026

Search research articles

Related Experiment Video

Updated: Sep 28, 2025

Microdissection of Black Widow Spider Silk-producing Glands

Microdissection of Black Widow Spider Silk-producing Glands

Published on: January 11, 2011

Complexity of Spider Dragline Silk.

Ali D Malay¹, Hamish C Craig¹, Jianming Chen¹

¹Biomacromolecules Research Team, Center for Sustainable Resource Science, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.

Biomacromolecules

|April 4, 2022

Summary

Scientists are exploring the complex composition of spider dragline silk to create advanced smart materials. Understanding the intricate protein structures and self-assembly is key to mimicking nature's toughest fibers.

More Related Videos

Synthetic Spider Silk Production on a Laboratory Scale

Synthetic Spider Silk Production on a Laboratory Scale

Published on: July 18, 2012

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure

Published on: May 6, 2019

Related Experiment Videos

Last Updated: Sep 28, 2025

Microdissection of Black Widow Spider Silk-producing Glands

Microdissection of Black Widow Spider Silk-producing Glands

Published on: January 11, 2011

Synthetic Spider Silk Production on a Laboratory Scale

Synthetic Spider Silk Production on a Laboratory Scale

Published on: July 18, 2012

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure

Published on: May 6, 2019

Area of Science:

Biomaterials Science
Materials Engineering
Biochemistry

Background:

Spider dragline silk exhibits exceptional toughness, inspiring efforts to synthesize artificial versions.
Current artificial spider silk production often oversimplifies the natural spinning process.
This simplification may limit the mechanical properties of synthetic silk fibers.

Purpose of the Study:

To discuss recent findings on the complex material constituents of spider dragline silk.
To explore spidroin domain functions and self-assembly mechanisms.
To inform biomimetic approaches for artificial spider silk production.

Main Methods:

Review of recent scientific literature on spider silk composition and structure.
Analysis of spidroin subtypes, nonspidroin proteins, and post-translational modifications.
Consideration of biomolecular condensate frameworks for silk self-assembly.

Main Results:

Spider dragline silk composition is more complex than the traditional two-component model (MaSp1/MaSp2).
Novel spidroin subtypes and nonspidroin proteins contribute to silk properties.
Post-translational modifications may play a role in silk fiber formation.

Conclusions:

A deeper understanding of silk's intricate components is crucial for successful biomimetic material design.
Viewing silk self-assembly through biomolecular condensate principles offers new insights.
Further research into the complexity of natural silk can guide the development of superior artificial spider silk.