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Related Concept Videos

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

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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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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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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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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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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).
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Filovirus Filament Proteins.

Daniel R Beniac1, Lindsey L Lamboo1,2, Timothy F Booth3,4

  • 1Viral Diseases Division, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, MB, Canada.

Sub-Cellular Biochemistry
|June 15, 2018
PubMed
Summary

Filoviruses, causing hemorrhagic fevers, feature a flexible, double-layered nucleocapsid (NC) enabling diverse virion shapes. This unique structure may enhance viral replication and host cell invasion.

Keywords:
Filovirus ribonucleoproteinMatrix protein polymeraseMorphogenesisNucleocapsidVirus envelope

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Filoviruses are filamentous, enveloped viruses responsible for severe hemorrhagic fevers.
  • Their nucleocapsid (NC) is a complex structure with distinct inner and outer layers.

Purpose of the Study:

  • To elucidate the structural organization of the filovirus nucleocapsid (NC).
  • To understand how NC structure relates to filovirus morphology, flexibility, and replication.

Main Methods:

  • Analysis of the filovirus NC structure, including protein composition and arrangement.
  • Investigation of the relationship between NC structure and virion polymorphism.

Main Results:

  • The NC has a double-layered helical structure with NP-RNA complex and VP24-VP35 heterodimers.
  • Absence of vertical connections allows NC flexibility, enabling various virion shapes (linear, comma, toroidal).
  • VP40 forms a lattice layer, with a gap to the NC, maintaining axial alignment.

Conclusions:

  • Filovirus unique morphology, including NC flexibility and VP40 arrangement, likely contributes to high-titer replication, transmission, and broad host cell/tissue invasion.