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

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 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...
Forces Acting on Chromosomes02:11

Forces Acting on Chromosomes

During mitosis, chromosome movements occur through the interplay of multiple piconewton level forces. In prometaphase, these forces help in chromosome assembly or congression at the equatorial plane, eventually leading to their alignment at the metaphase plate. The forces acting on the chromosomes are space and time-dependent; therefore, they vary with the position of the chromosomes as the cell progresses through mitosis. 
Microtubules and motor proteins exert two types of forces on...
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...
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...

You might also read

Related Articles

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

Sort by
Same author

De novo assembly and single-molecule study of kinetochore-microtubule interactions.

Frontiers in cell and developmental biology·2026
Same author

Separating chromosomes, one way or another.

The Journal of cell biology·2025
Same author

Direct observation of interdependent and hierarchical kinetochore assembly on individual centromeres.

Nucleic acids research·2025
Same author

Direct observation of interdependent and hierarchical kinetochore assembly on individual centromeres.

bioRxiv : the preprint server for biology·2025
Same author

Centromeres in the thermotolerant yeast K. marxianus mediate attachment to a single microtubule.

Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology·2025
Same author

Centromeres in the thermotolerant yeast K. marxianus mediate attachment to a single microtubule.

Research square·2025

Related Experiment Video

Updated: Jul 9, 2026

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
08:04

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

Kinesin steps do not alternate in size.

Adrian N Fehr, Charles L Asbury, Steven M Block

    Biophysical Journal
    |December 18, 2007
    PubMed
    Summary
    This summary is machine-generated.

    Kinesin motor proteins move along microtubules in uniform 8-nm steps. Analysis of single-molecule traces revealed consistent step sizes, constraining models of kinesin

    More Related Videos

    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

    Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins
    07:25

    Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

    Published on: October 17, 2014

    Related Experiment Videos

    Last Updated: Jul 9, 2026

    Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
    08:04

    Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

    Published on: January 26, 2019

    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

    Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins
    07:25

    Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

    Published on: October 17, 2014

    Area of Science:

    • Cellular biology
    • Biophysics
    • Molecular motors

    Background:

    • Kinesin is a crucial motor protein for intracellular transport.
    • Its step-wise movement along microtubules is essential for cellular function.
    • The precise step size and trajectory of kinesin remain debated, with models proposing uniform or alternating step sizes.

    Discussion:

    • Analysis of single-molecule stepping traces from "limping" kinesin provided insights into individual head movements.
    • Distinguishing fast and slow phases allowed for the calculation of step sizes for each kinesin head.
    • Comparison with non-limping kinesin data validated the findings.

    Key Insights:

    • Kinesin exhibits uniform 8-nm steps during its movement along microtubules.
    • This finding refutes models predicting alternating step sizes (7-nm and 9-nm).
    • The uniform step size provides strong constraints for future kinesin mechanism models.

    Outlook:

    • Further research can explore how this uniform stepping mechanism is regulated.
    • Investigating variations in step size across different kinesin family members.
    • Understanding the implications of uniform 8-nm steps for cargo transport efficiency.