Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
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...
Microtubules in Cell Motility01:24

Microtubules in Cell Motility

Microtubules are thick hollow cylindrical proteins that help form the cytoskeleton. Microtubules have varied roles in the cell. These filaments help form cellular appendages like cilia and flagella, which are responsible for locomotion. The cilia arise from basal bodies, separated from the main body by a membrane-like structure forming the transition zone. This zone is the gate for the entry of lipids and proteins, creating a unique composition of lipids and proteins in the ciliary membrane and...
Microtubules in Cell Motility01:24

Microtubules in Cell Motility

Microtubules are thick hollow cylindrical proteins that help form the cytoskeleton. Microtubules have varied roles in the cell. These filaments help form cellular appendages like cilia and flagella, which are responsible for locomotion. The cilia arise from basal bodies, separated from the main body by a membrane-like structure forming the transition zone. This zone is the gate for the entry of lipids and proteins, creating a unique composition of lipids and proteins in the ciliary membrane and...
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,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Structural diversity and unity amongst axonemal dynein assembly factors.

Journal of cell science·2025
Same author

Post-LECA Origin and Diversification of an Axonemal Outer Arm Dynein Motor.

Cytoskeleton (Hoboken, N.J.)·2025
Same author

Cilia biology: Building the central pair apparatus tip.

Current biology : CB·2025
Same author

Isoform-specific phosphorylation of axonemal dynein heavy chains.

Molecular biology of the cell·2025
Same author

Steric Complementarity Drives Strong Co-Assembly of Short Peptide Stereoisomers.

Journal of the American Chemical Society·2025
Same author

<i>Chlamydomonas</i> FBB18 is a ubiquitin-like protein essential for the cytoplasmic preassembly of various ciliary dyneins.

Proceedings of the National Academy of Sciences of the United States of America·2025

Related Experiment Video

Updated: May 12, 2026

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets
10:52

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets

Published on: August 13, 2016

A solid-state control system for dynein-based ciliary/flagellar motility.

Stephen M King1

  • 1Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030, USA. king@neuron.uchc.edu

The Journal of Cell Biology
|April 10, 2013
PubMed
Summary
This summary is machine-generated.

Researchers identified the MIA complex in Chlamydomonas reinhardtii, linking regulatory structures to inner arm dynein. This complex is crucial for coordinating ciliary and flagellar beating and determining waveform.

More Related Videos

Single-Molecule Analysis of Sf9 Purified Superprocessive Kinesin-3 Family Motors
08:16

Single-Molecule Analysis of Sf9 Purified Superprocessive Kinesin-3 Family Motors

Published on: July 27, 2022

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells
10:46

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells

Published on: February 2, 2022

Related Experiment Videos

Last Updated: May 12, 2026

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets
10:52

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets

Published on: August 13, 2016

Single-Molecule Analysis of Sf9 Purified Superprocessive Kinesin-3 Family Motors
08:16

Single-Molecule Analysis of Sf9 Purified Superprocessive Kinesin-3 Family Motors

Published on: July 27, 2022

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells
10:46

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells

Published on: February 2, 2022

Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Motors

Background:

  • Ciliary and flagellar motility depend on the precise coordination of various dynein motor proteins.
  • Dynein motors possess diverse enzymatic and mechanical characteristics essential for generating flagellar and ciliary beating patterns.

Purpose of the Study:

  • To identify novel protein complexes involved in the regulation of ciliary and flagellar function.
  • To elucidate the molecular mechanisms connecting regulatory structures to motor proteins in the axoneme.

Main Methods:

  • Proteomic analysis of the Chlamydomonas reinhardtii axoneme.
  • Biochemical assays to determine protein-protein interactions.
  • In vivo imaging and functional assays to assess the role of identified complexes.

Main Results:

  • Identification of the MIA (modifier of inner arms) complex within the Chlamydomonas reinhardtii axoneme.
  • Demonstration that the MIA complex physically links radial spokes to an inner arm dynein.
  • Evidence for the MIA complex acting as a signaling conduit.

Conclusions:

  • The MIA complex is a key component in the regulatory pathway controlling ciliary and flagellar waveform.
  • This finding provides new insights into the intricate signaling networks governing microtubule-based motor function.