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Related Concept Videos

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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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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Introduction to Actin01:26

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Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
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Formation of Higher-order Actin Filaments01:11

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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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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.
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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation
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Dynactin 3D structure: implications for assembly and dynein binding.

Hiroshi Imai1, Akihiro Narita2, Yuichiro Maéda3

  • 1ERATO Actin Filament Dynamics Project, Japan Science and Technology Agency, c/o RIKEN, Sayo, Hyogo 679-5148, Japan; Laboratory for Structural Biochemistry, RIKEN Harima Institute SPring-8 Center, Sayo, Hyogo 679-5148, Japan.

Journal of Molecular Biology
|July 22, 2014
PubMed
Summary
This summary is machine-generated.

This study reveals the 3D structure of native dynactin, a key component of the dynein motor. The structure clarifies dynactin assembly and dynein binding mechanisms.

Keywords:
3D EMactindyneinmicrotubulesingle particle analysis

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Dynactin is a crucial multisubunit complex for cytoplasmic dynein motor function.
  • Previous structural studies were limited to small fragments, hindering understanding of the full ≈1MDa assembly.

Purpose of the Study:

  • To determine the high-resolution three-dimensional (3D) structure of native vertebrate dynactin.
  • To elucidate the assembly mechanism and length specification of dynactin.

Main Methods:

  • Negative-stain electron microscopy (EM).
  • Image analysis using random conical tilt reconstruction.
  • Molecular fitting of actin-related protein (Arp) polymers into the EM density envelope.

Main Results:

  • A detailed 3D structure of the 35-nm dynactin molecule was obtained, revealing a V-shaped shoulder and a flattened tip.
  • The structure provides insights into dynein binding mechanisms and the helical parameters of the Arp filament core.
  • The Arp filament core contains 7-9 Arp protomers, with the 7 Arp model best fitting observed stoichiometry and structural data.

Conclusions:

  • The determined 3D structure provides a framework for understanding dynactin assembly and length regulation.
  • The findings offer new perspectives on the interaction between dynactin and the dynein motor complex.
  • This work advances the structural understanding of essential cellular machinery.