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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,...
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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...
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A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker proteins that...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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Anaphase A and B01:39

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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.
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Related Experiment Video

Updated: Jun 30, 2026

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
08:04

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

Processive kinesins require loose mechanical coupling for efficient collective motility.

Peter Bieling1, Ivo A Telley, Jacob Piehler

  • 1Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.

EMBO Reports
|September 20, 2008
PubMed
Summary
This summary is machine-generated.

Processive motor proteins like kinesin-1 can interfere with each other when working together. Loose mechanical coupling, facilitated by kinesin-1

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Last Updated: Jun 30, 2026

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08:04

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Published on: May 10, 2022

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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:

  • Biophysics
  • Molecular Motor Function
  • Cellular Transport

Background:

  • Processive motor proteins, such as kinesin-1, exhibit stochastic stepping behavior, meaning they only take mechanical steps for a fraction of their bound time.
  • Motor proteins often function collectively in teams, raising questions about potential interference due to mechanical coupling and individual motor stochasticity.

Purpose of the Study:

  • To quantitatively investigate how mechanical coupling between kinesin-1 motors affects the efficiency of collective microtubule transport.
  • To determine the role of kinesin-1's non-motor regions in mediating or mitigating interference within motor ensembles.

Main Methods:

  • Immobilization of processive kinesin-1 motors at controlled surface densities on biocompatible surfaces.
  • Quantitative analysis of collective microtubule transport dynamics under varying motor densities and motor constructs.
  • Development and application of a mathematical model incorporating known physical properties of individual kinesin-1 molecules.

Main Results:

  • Kinesin-1 constructs lacking significant non-motor sequences exhibited reduced collective transport speed, demonstrating negative interference dependent on the number of interacting motors.
  • The observed negative interference in motor ensembles was quantitatively explained by a mathematical model based on individual kinesin-1 molecular properties.
  • The non-motor extension of kinesin-1 was found to reduce this mutual interference between motors.

Conclusions:

  • Stochastic stepping of individual motors can lead to negative interference when kinesin-1 motors are tightly mechanically coupled.
  • Efficient collective transport by kinesin-1 ensembles requires loose mechanical coupling, which is facilitated by the motor's non-motor regions.