Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

The Movement of Organelles and Vesicles

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 Proteins

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...

Anaphase A and B

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...

Actin and Myosin in Muscle Contraction

Actin and Myosin in Muscle Contraction

Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...

Microtubules in Cell Motility

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 Motility

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

Bile-mediated ToxS homodimerization provides a model for ToxRS periplasmic interactions.

bioRxiv : the preprint server for biology·2026

Same author

Mechanical states of a motor protein in the spindle.

Current biology : CB·2026

Same author

Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.

Scientific reports·2026

Same author

Characterization of the ligand binding pocket of the virulence regulator Rns, a member of the AraC/XylS family of transcription factors.

mSphere·2025

Same author

<i>Vibrio cholerae</i> CsrA controls ToxR levels by increasing the stability and translation of <i>toxR</i> mRNA.

mBio·2024

Same author

<i>Vibrio cholerae</i> CsrA controls ToxR levels by increasing the stability and translation of <i>toxR</i> mRNA.

bioRxiv : the preprint server for biology·2024

Search research articles

Related Experiment Video

Updated: Jun 11, 2026

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

A kinesin motor in a force-producing conformation.

Elisabeth Heuston¹, C Eric Bronner, F Jon Kull

¹Department of Chemistry, Dartmouth College, Hanover, NH 03755, USA.

BMC Structural Biology

|July 7, 2010

Summary

Mutation in kinesin-14 Ncd motor uncouples ATP hydrolysis from force generation. The C-terminus docking mechanism explains force production in minus-end kinesin motors.

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Kinesin motors convert chemical energy into mechanical work via ATP hydrolysis.
The precise mechanism and intermediate states of kinesin motor function remain poorly understood.
Point mutations can stabilize transient states for structural characterization.

Purpose of the Study:

To investigate the structural and functional consequences of a specific point mutation in kinesin-14 Ncd.
To elucidate the mechanism of force generation in Ncd motors.

Main Methods:

Site-directed mutagenesis of kinesin-14 Ncd.
In vitro gliding assays to measure microtubule motility.
X-ray crystallography to determine motor structure.

More Related Videos

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Published on: May 10, 2022

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

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

Published on: October 15, 2019

Related Experiment Videos

Last Updated: Jun 11, 2026

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Published on: May 10, 2022

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

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

Published on: October 15, 2019

Main Results:

A single point mutation in Ncd accelerated ATP hydrolysis but reduced microtubule gliding speed, uncoupling hydrolysis from force.
Crystal structure revealed a rotated stalk conformation and novel C-terminal interactions.
The C-terminus docked onto the motor core, forming a structure analogous to the kinesin-1 neck linker.

Conclusions:

Force generation in minus-end directed Ncd motors involves C-terminal docking, mimicking the kinesin-1 neck linker.
Both plus- and minus-end kinesin motors may utilize similar conformational changes for force production.
Unstable ADP binding likely triggers conformational changes leading to force generation in Ncd.