Filopodia Disassembly
Filopodia Disassembly - Related Videos
02:49
Detection of Biofilm Disassembly Through a Dispersion Assay
0 Views •
2025
The video showcases a biofilm dispersion assay using a multi-well plate. Buffer and glucose treatment disassemble the biofilm, releasing bacteria, while bile salts induce stress, retaining bacteria in the protective extracellular polymeric substance. Higher dispersion with buffer and glucose confirms successful biofilm disassembly, estimated by colony forming units measurement.
01:39
Mechanism of Filopodia Formation
0 Views •
2023
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...
01:35
Disassembly of Intermediate Filaments
0 Views •
2023
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...
07:24
In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
0 Views •
Cited by 4 •
2016
Disassembly of influenza A virus cores during virus entry into host cells is a multistep process. We describe an in vitro method to analyze the early stages of viral uncoating. In this approach, velocity gradient centrifugation is used to biochemically dissect the steps that initiate uncoating under defined conditions.
02:42
In Vitro Disassembly of the Influenza A Virus Core Using pH-Controlled Gradient Centrifugation
0 Views •
2026
Source: Stauffer, S. et al. In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation. J. Vis. Exp. (2016)This video demonstrates the pH-dependent disassembly of influenza A virus (IAV) cores using gradient ultracentrifugation. It outlines glycerol gradient preparation, ultracentrifugation, and how different pH conditions affect IAV core disassembly.
FAQs
Disassembly begins when actin filament loss exceeds filament assembly. Reduced polymerization, ongoing depolymerization, and actin turnover collectively shorten the filament core. As this balance changes, the protrusion can retract rather than remain extended, allowing the cell to modify its contact with the surrounding environment and redirect later shape or movement changes.
The tip is a critical site for maintaining filament length. When polymerization there decreases, new actin no longer offsets filament loss efficiently. Continued turnover can therefore produce shortening and retraction. This mechanism links local molecular changes at the protrusion tip with visible remodeling of the cell surface and its environmental contacts.
Disassembly is not controlled by actin turnover alone. Reorganization of the attachments connecting the membrane and cytoskeleton can alter how a protrusion is supported and maintained. When these connections are remodeled together with filament loss, the cell can dismantle the protrusion in a coordinated way rather than simply shortening isolated actin filaments.
Retraction removes or redirects protrusions that help a cell sense its surroundings. This can change the spatial pattern of environmental interactions, reshape the cell, and influence the direction of migration. Because protrusions also participate in contacts with neighboring cells or the extracellular matrix, their disassembly can modify adhesion-related behavior as well.
A useful analysis should follow changes in actin filament length, the balance between assembly and depolymerization, tip polymerization, and membrane–cytoskeleton attachments. Researchers can then relate these structural changes to protrusion retraction, cell shape, migration direction, or altered contacts. Connecting molecular turnover with cellular outcomes helps reveal how cytoskeletal dynamics regulate behavior.
These settings depend on controlled changes in cell movement, guidance, shape, or interactions with surrounding structures. Studying protrusion disassembly therefore provides a way to investigate how cytoskeletal remodeling contributes to those processes. Its relevance extends from wound healing and neuronal growth to disease biology, where altered regulation of cellular contacts or movement may be important.