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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,...
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

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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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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
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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...
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Related Experiment Video

Updated: Jun 25, 2026

Single-Molecule Analysis of Sf9 Purified Superprocessive Kinesin-3 Family Motors
08:16

Single-Molecule Analysis of Sf9 Purified Superprocessive Kinesin-3 Family Motors

Published on: July 27, 2022

Dissection of kinesin's processivity.

Sarah Adio1, Johann Jaud, Bettina Ebbing

  • 1Physics Department E22, Technical University Munich, Garching, Germany.

Plos One
|February 27, 2009
PubMed
Summary
This summary is machine-generated.

Kinesin motor proteins require coordinated heads for movement. Uncoupling motor domains shows that while spacing is important, specific motor head elements are crucial for kinesin stepping and processivity.

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Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
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Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

Area of Science:

  • Molecular motor proteins
  • Cellular transport mechanisms
  • Kinesin superfamily dynamics

Background:

  • Kinesins are microtubule-based motor proteins essential for intracellular transport.
  • Processive movement relies on coupled catalytic steps and mechanical coordination between the two motor heads.
  • Understanding the specific contributions of different kinesin domains is key to deciphering their motility mechanisms.

Purpose of the Study:

  • To investigate the functional roles of motor head domains versus dimerization domains in kinesin processivity.
  • To determine if spatial proximity of motor domains is sufficient for processive movement.
  • To elucidate the molecular requirements for coupling ATP hydrolysis to mechanical stepping in kinesin dimers.

Main Methods:

  • Construction and analysis of chimeric kinesin constructs combining domains from Kinesin-1 and Kinesin-3.
  • Utilizing Total Internal Reflection Fluorescence (TIRF) microscopy and bead motility assays to measure processive movement.
  • Biochemical assays to monitor nucleotide exchange (ATP binding and ADP release) in the chimeric proteins.

Main Results:

  • A chimera with Kinesin-1 motor domains and Kinesin-3 dimerization domains exhibited processive motility, indicating sufficient spatial proximity for Kinesin-1 function.
  • The reverse chimera, with non-processive Kinesin-3 motor domains, failed to step along microtubules, even with Kinesin-1 neck structures.
  • Despite impaired stepping, ATP binding in one head of the reverse chimera induced ADP release from the partner head, demonstrating preserved alternating site catalysis.

Conclusions:

  • Processive kinesin movement necessitates specific elements within the motor head that sense ADP release and initiate stepping.
  • Neck coiled-coil mediated spacing of motor heads is necessary but not sufficient for processivity.
  • The motor head's intrinsic properties, beyond mere proximity, are critical for coordinating mechanical steps and achieving sustained directional movement along microtubules.