Jove
Visualize
Contact Us

Related Concept Videos

Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

2.9K
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...
2.9K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.0K
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...
2.0K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

18.1K
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...
18.1K
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

1.8K
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.
1.8K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.3K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.3K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

2.9K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
2.9K

You might also read

Related Articles

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

Sort by
Same author

Stress-relaxing granular bioprinting materials enable complex and uniform organoid self-organization.

Nature materials·2026
Same author

Bioenergetic responses to β-adrenergic stimulation in beige adipocyte depend on actomyosin driven forces.

bioRxiv : the preprint server for biology·2025
Same author

POMPOMS: Crosslinked Biomolecular Condensates as a Versatile Platform for Multifunctional Protein Microparticles.

Biomacromolecules·2025
Same author

POMPOMS: Crosslinked biomolecular condensates as a versatile platform for multifunctional protein microparticles.

bioRxiv : the preprint server for biology·2025
Same author

Frequency-dependent cellular microrheology with pyramidal atomic force microscopy probes.

bioRxiv : the preprint server for biology·2025
Same author

Understanding long-range opposite charge repulsion in multivalent salt solutions.

The Journal of chemical physics·2024
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Video

Updated: Jun 6, 2025

Self-Assembly of Microtubule Tactoids
08:49

Self-Assembly of Microtubule Tactoids

Published on: June 23, 2022

3.8K

Dissecting neurofilament tail sequence-phosphorylation-structure relationships with multicomponent reconstituted

Erika A Ding1, Takashi J Yokokura1, Rui Wang1,2

  • 1Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA 94720.

Proceedings of the National Academy of Sciences of the United States of America
|November 27, 2024
PubMed
Summary

Neurofilament (NF) tail protein constructs were studied to understand their brush conformation. NF-Medium (NFM) and NF-Heavy (NFH) brushes show complex morphologies influenced by charge and phosphorylation.

Keywords:
cytoskeletonintrinsically disordered proteinsneurofilaments

More Related Videos

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

18.7K
Purification of the Dendritic Filopodia-rich Fraction
11:51

Purification of the Dendritic Filopodia-rich Fraction

Published on: May 2, 2019

5.2K

Related Experiment Videos

Last Updated: Jun 6, 2025

Self-Assembly of Microtubule Tactoids
08:49

Self-Assembly of Microtubule Tactoids

Published on: June 23, 2022

3.8K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

18.7K
Purification of the Dendritic Filopodia-rich Fraction
11:51

Purification of the Dendritic Filopodia-rich Fraction

Published on: May 2, 2019

5.2K

Area of Science:

  • Biophysics
  • Cell Biology
  • Neuroscience

Background:

  • Neurofilaments (NFs) are key axonal cytoskeleton components with intrinsically disordered tail domains.
  • The conformation and function of NF tail brushes, influenced by charge and phosphorylation, are not fully understood.

Purpose of the Study:

  • To investigate how neurofilament tail protein constructs (NFL, NFM, NFH) form protein brushes.
  • To determine the impact of composition, phosphorylation, and charge patterns on brush conformation and morphology.

Main Methods:

  • Grafting recombinant NF tail proteins (NFL, NFM, NFH) onto surfaces to create defined protein brushes.
  • Atomic force microscopy (AFM) to measure brush height and morphology.
  • Self-consistent field theory (SCFT) modeling to predict and analyze brush structures.

Main Results:

  • Brush height depends monotonically but not always linearly on composition.
  • NFM brushes are highly extended; NFH brushes are compact despite phosphorylation.
  • SCFT predicts multilayer morphologies for NFM and phosphorylated NFH brushes, driven by N-terminal charges in NFH and charge segregation in NFM.

Conclusions:

  • NF-M plays a role in the dynamic range of NF brush conformation.
  • NFH tail N-terminal charges and C-terminal regions influence multilayer formation and height.
  • Disordered protein sequence contributions to interfacial conformation can be dissected using this platform.