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Related Concept Videos

Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
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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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Microtubules in Cell Motility01:24

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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 Motility01:24

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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...
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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...

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Development of a Microfluidics-Based Approach for Investigating Microtubule Polymer Mechanics
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FLUCTUATING MOTOR FORCES BEND GROWING MICROTUBULES.

Nandini Shekhar1, Srujana Neelam, Jun Wu

  • 1Department of Chemical Engineering, University of Florida, Gainesville, FL 32611, USA.

Cellular and Molecular Bioengineering
|September 17, 2013
PubMed
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Growing microtubules bend due to non-thermal forces. Dynein motor proteins, not just thermal energy, generate these forces, significantly impacting microtubule dynamics and cellular structure.

Keywords:
Microtubule bendingdyneinmyosin

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Area of Science:

  • Cell Biology
  • Biophysics
  • Cytoskeleton Dynamics

Background:

  • Microtubules are rigid cytoskeletal polymers essential for cell structure and division.
  • Growing microtubule tips exhibit significant bending beyond thermal fluctuations, suggesting unknown forces.
  • Identifying the source of these non-thermal forces is crucial for understanding microtubule dynamics.

Purpose of the Study:

  • To investigate the source of non-thermal forces responsible for bending growing microtubules.
  • To determine the roles of motor proteins, specifically dynein and myosin, in microtubule tip bending.

Main Methods:

  • Live-cell imaging of microtubule polymerization dynamics in NIH-3T3 fibroblasts.
  • Utilizing EGFP-EB1, a fluorescent marker for growing microtubule plus-ends (+TIPs).
  • Pharmacological inhibition of dynein and myosin motor proteins to assess their impact on microtubule tip motion.

Main Results:

  • Dynein inhibition markedly reduced the deviation of growing microtubule tips from their initial paths.
  • Myosin inhibition showed a modest decrease in microtubule tip fluctuations.
  • Combined inhibition of dynein and myosin did not further reduce fluctuations compared to dynein inhibition alone.

Conclusions:

  • Dynein motor proteins are key contributors to the non-thermal forces that bend growing microtubules.
  • These forces are generated and transmitted through dynein linkages, influencing microtubule polymerization and cellular mechanics.
  • The findings provide a new model for understanding forces acting on the dynamic microtubule cytoskeleton.