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Related Concept Videos

Mechanism of Ciliary Motion01:05

Mechanism of Ciliary Motion

The ciliary structures were first seen in 1647 by Antonie Leeuwenhoek while observing the protozoans. In lower organisms, these appendages are responsible for cell movement, while in higher organisms, these appendages help in the movement of the extracellular fluids within the body cavities.
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular cargos...
The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Disassembly of Intermediate Filaments01:35

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...
Anaphase A and B01:39

Anaphase A and B

Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...

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Related Experiment Video

Updated: May 22, 2026

Quantifying Cytoskeleton Dynamics Using Differential Dynamic Microscopy
06:37

Quantifying Cytoskeleton Dynamics Using Differential Dynamic Microscopy

Published on: June 15, 2022

Dynein dynamics.

Peter Höök1, Richard Vallee

  • 1Department of Pathology and Cell Biology, Columbia University College of Physicians and Surgeons, New York, New York, USA.

Nature Structural & Molecular Biology
|May 4, 2012
PubMed
Summary

Dyneins, the largest cytoskeletal motor proteins, exhibit complex mechanochemical behavior. New crystallographic data reveal surprising motor domain structures, offering fresh insights into force generation and movement mechanisms.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Dyneins are crucial cytoskeletal motor proteins responsible for intracellular transport.
  • Their complex mechanochemical cycle governs force generation and movement.

Purpose of the Study:

  • To elucidate the structural basis of dynein motor function.
  • To understand the mechanisms of force production and movement in dyneins.

Main Methods:

  • High-resolution crystallography
  • Structural analysis of dynein motor domains

Main Results:

  • Revealed novel structural organization within the dynein motor domain.
  • Provided new insights into the molecular mechanisms underlying force generation.

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Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation
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Analysis of Actomyosin Dynamics at Local Cellular and Tissue Scales Using Time-lapse Movies of Cultured Drosophila Egg Chambers
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Analysis of Actomyosin Dynamics at Local Cellular and Tissue Scales Using Time-lapse Movies of Cultured Drosophila Egg Chambers

Published on: June 3, 2019

Related Experiment Videos

Last Updated: May 22, 2026

Quantifying Cytoskeleton Dynamics Using Differential Dynamic Microscopy
06:37

Quantifying Cytoskeleton Dynamics Using Differential Dynamic Microscopy

Published on: June 15, 2022

Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation
08:09

Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation

Published on: October 15, 2019

Analysis of Actomyosin Dynamics at Local Cellular and Tissue Scales Using Time-lapse Movies of Cultured Drosophila Egg Chambers
10:45

Analysis of Actomyosin Dynamics at Local Cellular and Tissue Scales Using Time-lapse Movies of Cultured Drosophila Egg Chambers

Published on: June 3, 2019

  • Offered a deeper understanding of how dyneins achieve movement.
  • Conclusions:

    • Recent structural studies have unveiled unexpected features of dynein motor organization.
    • These findings advance our comprehension of dynein's mechanochemical cycle and motor function.