Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Destabilization of Microtubules01:45

Destabilization of Microtubules

3.2K
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...
3.2K
Drugs that Stabilize Microtubules01:15

Drugs that Stabilize Microtubules

2.4K
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...
2.4K
Drugs that Destabilize Microtubules01:10

Drugs that Destabilize Microtubules

2.2K
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...
2.2K
Microtubule Instability02:17

Microtubule Instability

5.6K
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...
5.6K
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

5.4K
Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
5.4K
Anaphase A and B01:39

Anaphase A and B

4.8K
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...
4.8K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.

bioRxiv : the preprint server for biology·2026
Same author

Evaluating the Performance of Photon- and Electron-Based Fragmentation Methods in Omnitrap-LCMS Analysis of <i>N</i>-Glycopeptides.

Analytical chemistry·2026
Same author

Spatial distribution of the proteome in the human body and in cancers.

Nature·2026
Same author

Taxol exploits molecular switches within tubulin to stabilize microtubules.

bioRxiv : the preprint server for biology·2026
Same author

Capping protein dynamics are defined by the stalk and restricted by CPI-motif and V-1 binding.

Biophysical journal·2026
Same author

The inner nuclear membrane protein SUN1 regulates cullin-3 neddylation to maintain insulin signaling.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Nov 20, 2025

Quantitative Microtubule Fractionation Technique to Separate Stable Microtubules, Labile Microtubules, and Free Tubulin in Mouse Tissues
07:21

Quantitative Microtubule Fractionation Technique to Separate Stable Microtubules, Labile Microtubules, and Free Tubulin in Mouse Tissues

Published on: November 17, 2023

2.3K

Parthenolide Destabilizes Microtubules by Covalently Modifying Tubulin.

Takashi Hotta1, Sarah E Haynes2, Teresa L Blasius1

  • 1Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.

Current Biology : CB
|January 22, 2021
PubMed
Summary

Parthenolide, thought to inhibit microtubule detyrosination, actually causes tubulin aggregation. A new inhibitor, epoY, effectively blocks detyrosination, offering a precise tool for studying this vital post-translational modification.

Keywords:
detyrosinationepoYparthenolidetubulinvasohibin

More Related Videos

Spatiotemporal Subcellular Manipulation of the Microtubule Cytoskeleton in the Living Preimplantation Mouse Embryo using Photostatins
08:13

Spatiotemporal Subcellular Manipulation of the Microtubule Cytoskeleton in the Living Preimplantation Mouse Embryo using Photostatins

Published on: November 30, 2021

2.7K
Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
12:20

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

Published on: March 15, 2014

14.7K

Related Experiment Videos

Last Updated: Nov 20, 2025

Quantitative Microtubule Fractionation Technique to Separate Stable Microtubules, Labile Microtubules, and Free Tubulin in Mouse Tissues
07:21

Quantitative Microtubule Fractionation Technique to Separate Stable Microtubules, Labile Microtubules, and Free Tubulin in Mouse Tissues

Published on: November 17, 2023

2.3K
Spatiotemporal Subcellular Manipulation of the Microtubule Cytoskeleton in the Living Preimplantation Mouse Embryo using Photostatins
08:13

Spatiotemporal Subcellular Manipulation of the Microtubule Cytoskeleton in the Living Preimplantation Mouse Embryo using Photostatins

Published on: November 30, 2021

2.7K
Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
12:20

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

Published on: March 15, 2014

14.7K

Area of Science:

  • Cell Biology
  • Biochemistry
  • Post-Translational Modifications

Background:

  • Detyrosination of α-tubulin is a crucial microtubule post-translational modification (PTM) with significant roles in cellular processes.
  • The enzyme complex VASH1/2-SVBP responsible for detyrosination was recently identified, limiting prior genetic studies.
  • Parthenolide, a natural product, has been widely used to inhibit detyrosination, but its precise mechanism was unclear.

Purpose of the Study:

  • To investigate the mechanism by which parthenolide affects α-tubulin detyrosination.
  • To evaluate parthenolide's direct effect on VASH1/2-SVBP activity.
  • To identify and validate a specific inhibitor for microtubule detyrosination.

Main Methods:

  • Mass spectrometry to detect parthenolide adducts on tubulin.
  • In vitro assays to assess VASH1/2-SVBP inhibition.
  • Cellular experiments to evaluate the effects of parthenolide and epoY on microtubule detyrosination and tubulin polymerization.

Main Results:

  • Parthenolide forms covalent adducts with cysteine and histidine residues on tubulin, leading to protein aggregation and impaired microtubule formation.
  • Parthenolide does not inhibit VASH1/2-SVBP activity in vitro.
  • EpoY, an epoxide inhibitor, effectively blocks microtubule detyrosination in cells.

Conclusions:

  • Parthenolide is a promiscuous inhibitor that indirectly affects detyrosination by disrupting tubulin polymerization.
  • EpoY serves as a specific and effective chemical inhibitor for studying microtubule detyrosination.
  • The findings necessitate a re-evaluation of previous studies relying on parthenolide to investigate detyrosination functions.