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Related Concept Videos

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...
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...
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...
Spindle Assembly02:50

Spindle Assembly

Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a microtubule array...

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Related Experiment Video

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

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Published on: March 15, 2014

Kinesin-8 motors act cooperatively to mediate length-dependent microtubule depolymerization.

Vladimir Varga1, Cecile Leduc, Volker Bormuth

  • 1Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.

Cell
|September 22, 2009
PubMed
Summary

Kinesin-8 motor proteins, like Kip3p, depolymerize microtubules based on length. A cooperative bumping mechanism at the plus end controls microtubule disassembly, ensuring proper organelle length.

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Related Experiment Videos

Last Updated: Jun 20, 2026

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

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Published on: March 15, 2014

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles
07:47

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

Published on: May 10, 2022

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
08:04

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

Area of Science:

  • Cell Biology
  • Molecular Motors
  • Cytoskeleton Dynamics

Background:

  • Kinesin-8 family motor proteins regulate microtubule dynamics.
  • Length-dependent microtubule depolymerization is critical for processes like mitotic spindle organization.
  • The precise mechanism of kinesin-8 mediated length-dependent depolymerization remains largely unelucidated.

Purpose of the Study:

  • To elucidate the single-molecule mechanism of length-dependent microtubule depolymerization by the kinesin-8 motor protein Kip3p from budding yeast.
  • To understand how Kip3p binding and dissociation at the microtubule plus end contribute to length regulation.

Main Methods:

  • Single-molecule microscopy was employed to observe the behavior of individual Kip3p molecules on microtubules.
  • Tracking of motor protein movement, binding, pausing, and dissociation events at microtubule plus ends was performed.

Main Results:

  • Kip3p motors bind microtubules and move to the plus end.
  • Individual Kip3p molecules pause at the plus end until displaced by incoming motors.
  • Dissociation of Kip3p results in the removal of a small number of tubulin dimers (1-2 on average).
  • Depolymerization rate is proportional to motor flux, explaining length-dependent disassembly.

Conclusions:

  • A cooperative motor-bumping mechanism at the microtubule plus end drives length-dependent depolymerization.
  • This feedback loop between motor flux and microtubule disassembly provides a model for molecular length sensing and control.
  • The findings offer insights into how cellular structures like the mitotic spindle are precisely regulated in length.