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

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...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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...
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...
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...
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...

You might also read

Related Articles

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

Sort by
Same author

Gene Therapy for Infants and Children With Otoferlin-Related Auditory Neuropathy Spectrum Disorder.

Ear and hearing·2026
Same author

Effect of contact needle technique on cancer-related fatigue in palliative care patients: a randomized controlled trial.

Supportive care in cancer : official journal of the Multinational Association of Supportive Care in Cancer·2026
Same author

Establishing functional giant Dictyostelium cells reveals front-rear polarity in intracellular signaling.

Communications biology·2026
Same author

Proliferation of a bloom-forming phytoplankton via uptake of polyphosphate-accumulating bacteria under phosphate-limiting conditions.

ISME communications·2025
Same author

Analysis of Adverse Events in Acupuncture and Moxibustion Treatments in Japan and the Current Situation of Hiroshima University Hospital Kampo Clinical Center.

Medical acupuncture·2025
Same author

Dexamethasone-eluting cochlear implants reduce inflammation and foreign body response in human and murine cochleae.

Scientific reports·2025

Related Experiment Video

Updated: Jun 27, 2026

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles
07:47

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Published on: May 10, 2022

Dynein pulls microtubules without rotating its stalk.

Hironori Ueno1, Takuo Yasunaga, Chikako Shingyoji

  • 1Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology (AIST), Higashi, Tsukuba, Ibaraki 305-8562, Japan.

Proceedings of the National Academy of Sciences of the United States of America
|December 10, 2008
PubMed
Summary

Sea urchin outer arm dynein uses its stalk as a grappling hook, not a lever arm, to move microtubules. This discovery challenges existing models of motor protein function in cilia and flagella motility.

More Related Videos

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

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
12:20

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends

Published on: March 15, 2014

Related Experiment Videos

Last Updated: Jun 27, 2026

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles
07:47

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Published on: May 10, 2022

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

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
12:20

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends

Published on: March 15, 2014

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Dynein is a crucial microtubule motor protein responsible for the motility of cilia and flagella.
  • Existing models propose dynein's stalk acts as a lever arm, amplifying conformational changes in the motor domain for microtubule sliding.

Purpose of the Study:

  • To visualize and analyze the action of dynein stalks bound to microtubules.
  • To elucidate the mechanical mechanism by which dynein generates force and movement.

Main Methods:

  • Utilized a novel
  • cryo-positive stain
  • electron microscopy technique.
  • Observed sea urchin outer arm dynein molecules bound to microtubules.
  • Performed in vitro motility assays to confirm dynein activity.

Main Results:

  • Provided the clearest images to date of dynein stalks interacting with microtubules.
  • Found no significant change in stalk angle between ADP.vanadate and no-nucleotide states.
  • Observed shifts in head and stalk positions relative to A-tubule attachments, contradicting lever arm models.

Conclusions:

  • Dynein's stalk functions as a grappling hook, not a lever arm, to engage tubulin subunits.
  • A novel mechanism is proposed where dynein retracts its tail (linker) to pull microtubules.
  • These findings offer new insights into the fundamental mechanics of microtubule-based motor proteins.