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Related Concept Videos

Drugs that Stabilize Microtubules01:15

Drugs that Stabilize Microtubules

Microtubules are dynamic structures that undergo cycles of catastrophe and rescue. The microtubules play a central role in cell division by forming the spindle apparatus for segregating the chromosomes. This makes them ideal targets for regulating dividing cells in tumors and malignant cancer cells. Microtubule stabilizing drugs help stabilize the microtubule formation and promote its polymerization. Paclitaxel was the first microtubule stabilizing agent used as anticancer drug in chemotherapy...
Drugs that Destabilize Microtubules01:10

Drugs that Destabilize Microtubules

Microtubules are dynamic structures and can be regulated by microtubule targeting agents (MTAs). Microtubule destabilizing drugs are a class of MTAs that destabilize and prevent microtubules' polymerization. Both natural and synthetic chemicals can be found under this class of drugs. Vincristine and vinblastine, two vinca alkaloids, and colchicine were among the first to be discovered. These drugs can affect cells in various ways, either by inducing a change in cell morphology, preventing...
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...
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...
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...

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Tiny Yeast Comet 1-Dependent Polymers Suppress Taxol-Stabilized Microtubule Depolymerization Induced by Ice-Cold

Scott C Schuyler1,2,3, Hsin-Yu Chen1, Cheng-Ye Weng1,3

  • 1Department of Biomedical Sciences, College of Medicine, Chang Gung University, Kwei-Shan, Taoyuan 333, Taiwan.

International Journal of Molecular Sciences
|June 26, 2026
PubMed
Summary

Budding yeast Tiny Yeast Comet 1 (Tyc1) forms polymers that associate with microtubules. These Tyc1p polymers can prevent microtubule breakdown, suggesting a role for human p31comet in microtubule dynamics.

Keywords:
Saccharomyces cerevisiaeTaxolTiny Yeast Comet 1 (Tyc1)cell division cycle 20 (Cdc20)electron microscopy (EM)microtubulemitotic-arrest deficient 2 (Mad2)p31comet

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Structural Biology

Background:

  • The protein Tiny Yeast Comet 1 (Tyc1) in budding yeast shares homology with human p31comet.
  • The conserved region in p31comet is known to bind microtubules.
  • p31comet structurally mimics the HORMA-domain protein Mad2, and other HORMA-domain proteins can form polymers.

Purpose of the Study:

  • To investigate the polymerization behavior of Tyc1p.
  • To determine the role of conserved motifs in Tyc1p polymerization.
  • To explore the functional implications of Tyc1p polymerization in microtubule stability.

Main Methods:

  • Negative staining electron microscopy was used to visualize Tyc1p polymers.
  • Tyc1p polymerization was studied in association with Taxol-stabilized microtubules.
  • Mutant forms of Tyc1p were analyzed to identify essential motifs for polymerization.

Main Results:

  • Tyc1p forms comet-tail-shaped polymers that associate with microtubules, often appearing braid-like.
  • Conserved amino acid motifs between Tyc1p and human p31comet are crucial for robust polymer formation.
  • Tyc1p polymers, in the presence of Mad2p, suppressed microtubule depolymerization induced by cold and CaCl2.

Conclusions:

  • Yeast Tyc1p forms polymers that stabilize microtubules.
  • These findings suggest a potential microtubule-associated function for human p31comet.
  • The study provides insights into the structural and functional roles of p31comet homologs in microtubule dynamics.