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Mechanism of Filopodia Formation

Mechanism of Filopodia Formation

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...

Formation of Intermediate Filaments

Formation of Intermediate Filaments

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 reported.

Generation of Straight or Branched Actin Filaments

Generation of Straight or Branched Actin Filaments

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...

Actin Filament Depolymerization

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...

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...

Fimbriae, Pili, and Axial Filaments

Fimbriae, Pili, and Axial Filaments

Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...

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Related Experiment Video

Updated: May 8, 2026

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

How do filovirus filaments bend without breaking?

Tim F Booth¹, Melissa J Rabb, Daniel R Beniac

¹National Microbiology Laboratory, Winnipeg, Canada; Department of Medical Microbiology, University of Manitoba, Winnipeg, Canada.

Trends in Microbiology

|September 10, 2013

Summary

This summary is machine-generated.

Mononegavirales viruses use flexible structures to protect their RNA genomes. This flexibility is key for replication and transcription in dangerous pathogens like Ebola virus.

Keywords:

Ebola virus cryo-electron microscopy filovirus nucleocapsid virus structure

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Last Updated: May 8, 2026

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

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Published on: May 5, 2022

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Measuring the Bending Stiffness of Bacterial Cells Using an Optical Trap

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Published on: April 26, 2010

Area of Science:

Virology
Structural Biology
Molecular Biology

Background:

Viruses in the order Mononegavirales possess helical nucleocapsids with single-stranded negative-sense RNA genomes.
This RNA-protein complex is essential for viral replication and transcription.
Recent structural data offers insights into filovirus functions, including dangerous pathogens like Ebola virus.

Purpose of the Study:

To review how the structure of filoviruses and paramyxoviruses allows for morphological flexibility.
To compare this flexibility to the rigid envelopes of rhabdoviruses.

Main Methods:

Review of recent structural data on Mononegavirales viruses.
Comparative analysis of viral structures (filoviruses, paramyxoviruses, rhabdoviruses).

Main Results:

Filoviruses have long, flexible filamentous viral envelopes accommodating multiple genome copies.
This flexibility prevents breakage of the large genomic RNA during infection.
Paramyxoviruses also exhibit flexibility, contrasting with the rigid envelopes of rhabdoviruses.

Conclusions:

Viral structure is critical for genome management and infectivity in Mononegavirales.
Morphological flexibility in filoviruses and paramyxoviruses is a key adaptation for their genomic material.
Understanding these structural adaptations is vital for studying viral pathogenesis and developing countermeasures.