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

Microtubule Instability02:17

Microtubule Instability

5.3K
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...
5.3K
Destabilization of Microtubules01:45

Destabilization of Microtubules

2.9K
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...
2.9K
Amyloid Fibrils03:03

Amyloid Fibrils

10.7K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
10.7K
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

4.8K
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...
4.8K

You might also read

Related Articles

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

Sort by
Same author

The critical role of the endogenous immune compartment after CAR T cell therapy in recurrent GBM.

Cell·2026
Same author

Altered hypothalamic functional connectivity in adolescents with severe obesity.

International journal of obesity (2005)·2026
Same author

Feasibility and pilot study protocol of the SURE programme: a co-designed whole-school approach intervention to promote migrant-background adolescents wellbeing in secondary education.

Pilot and feasibility studies·2026
Same author

Pituitary Apoplexy Precipitated by Non-Cranial Surgeries: An Institutional Experience.

Journal of neurological surgery. Part B, Skull base·2026
Same author

Tubulin C-terminal tails are pH sensors that regulate microtubule function.

bioRxiv : the preprint server for biology·2026
Same author

Role of α-tubulin helix 11' in heterodimer conformation and microtubule dynamics.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Oct 11, 2025

Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles
07:54

Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles

Published on: November 5, 2020

5.3K

Kinetically Stabilizing Mutations in Beta Tubulins Create Isotype-Specific Brain Malformations.

Kristen Park1, Katelyn J Hoff2, Linnea Wethekam2

  • 1Department of Pediatrics and Neurology, Children's Hospital Colorado, University of Colorado Anschutz Medical Campus, Aurora, CO, United States.

Frontiers in Cell and Developmental Biology
|December 6, 2021
PubMed
Summary

Mutations in beta-tubulin genes (TUBB2A, TUBB3) cause brain malformations. The T178M mutation stabilizes microtubules, disrupting GTPase activity crucial for brain development.

Keywords:
brain developmentcytoskeletonmicrotubuletubulintubulinopathy

More Related Videos

Label-Free Non-Linear Optics for the Study of Tubulin-Dependent Defects in Central Myelin
08:07

Label-Free Non-Linear Optics for the Study of Tubulin-Dependent Defects in Central Myelin

Published on: March 24, 2023

2.0K
A Novel Strategy Combining Array-CGH, Whole-exome Sequencing and In Utero Electroporation in Rodents to Identify Causative Genes for Brain Malformations
08:22

A Novel Strategy Combining Array-CGH, Whole-exome Sequencing and In Utero Electroporation in Rodents to Identify Causative Genes for Brain Malformations

Published on: December 1, 2017

8.7K

Related Experiment Videos

Last Updated: Oct 11, 2025

Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles
07:54

Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles

Published on: November 5, 2020

5.3K
Label-Free Non-Linear Optics for the Study of Tubulin-Dependent Defects in Central Myelin
08:07

Label-Free Non-Linear Optics for the Study of Tubulin-Dependent Defects in Central Myelin

Published on: March 24, 2023

2.0K
A Novel Strategy Combining Array-CGH, Whole-exome Sequencing and In Utero Electroporation in Rodents to Identify Causative Genes for Brain Malformations
08:22

A Novel Strategy Combining Array-CGH, Whole-exome Sequencing and In Utero Electroporation in Rodents to Identify Causative Genes for Brain Malformations

Published on: December 1, 2017

8.7K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Tubulinopathies result from mutations in tubulin genes, leading to brain malformations.
  • The precise impact of these mutations on tubulin function and distinct developmental outcomes remains unclear.

Purpose of the Study:

  • To investigate the functional consequences of T178M missense mutations in beta-tubulin genes (TUBB2A, TUBB3) associated with tubulinopathies.
  • To elucidate the role of tubulin GTPase activity in brain development.

Main Methods:

  • Analyzed RNA sequencing data of TUBB2A and TUBB3 expression in the brain.
  • Created and studied an analogous T178M mutation in yeast beta-tubulin.
  • Performed in vitro experiments with purified mutant tubulin.

Main Results:

  • Identified T178M mutations in TUBB2A or TUBB3 in patients with brain malformations.
  • Demonstrated that the T178M substitution kinetically stabilizes microtubules by slowing assembly/disassembly.
  • Showed that the mutation impairs GTPase-dependent conformational changes in tubulin.

Conclusions:

  • The T178M mutation disrupts essential GTPase activity of beta-tubulin, leading to kinetic stabilization of microtubules.
  • This mechanism provides insight into the pathogenesis of tubulinopathies.
  • Highlights the critical and differential roles of tubulin isotypes in brain development.