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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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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.
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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.
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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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The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
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The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
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Filament assemblies in foreign nucleic acid sensors.

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Helical assemblies are key in vertebrate innate immunity, detecting foreign DNA and RNA. This review details how RIG-I-like and AIM2-like receptors use helical structures to trigger immune responses.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Structural Biology

Background:

  • Helical filamentous assemblies are common in biological systems.
  • These structures are increasingly recognized for their role in the vertebrate innate immune system.
  • They are crucial for sensing foreign nucleic acids and initiating immune signaling.

Purpose of the Study:

  • To review the role of helical assemblies in the signaling pathways of RIG-I-like receptors (RLRs) and AIM2-like receptors (ALRs).
  • To describe ligand-dependent receptor oligomerization and its functional implications.
  • To explain receptor-dependent signaling adaptor oligomerization and its regulation.

Main Methods:

  • Review of existing scientific literature on helical assemblies in RLR and ALR signaling.
  • Analysis of mechanisms of ligand-dependent receptor oligomerization.
  • Examination of receptor-dependent oligomerization of signaling adaptors.

Main Results:

  • Helical oligomerization of RLRs and ALRs is essential for recognizing pathogen-associated molecular patterns (PAMPs) like foreign nucleic acids.
  • This oligomerization triggers downstream signaling cascades, leading to the production of antiviral and inflammatory mediators.
  • The process involves both ligand-induced receptor assembly and receptor-induced assembly of signaling adaptors.

Conclusions:

  • Helical assemblies are fundamental to innate immune sensing of nucleic acids via RLRs and ALRs.
  • Understanding these helical structures and their oligomerization provides insights into immune pathway activation and regulation.
  • Further research into these mechanisms can inform therapeutic strategies for inflammatory and antiviral responses.