Related Experiment Video
Updated: May 21, 2026

Extracting Modified Microtubules from Mammalian Cells to Study Microtubule-Protein Complexes by Cryo-Electron Microscopy
Published on: March 3, 2023
Genetically separable functions of the MEC-17 tubulin acetyltransferase affect microtubule organization
Irini Topalidou1, Charles Keller, Nereo Kalebic
1Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
Background:
Microtubules (MTs) are formed from the lateral association of 11-16 protofilament chains of tubulin dimers, with most cells containing 13-protofilament (13-p) MTs. How these different MTs are formed is unknown, although the number of protofilaments may depend on the nature of the α- and β-tubulins.
Results:
Here we show that the enzymatic activity of the Caenorhabiditis elegans α-tubulin acetyltransferase (α-TAT) MEC-17 allows the production of 15-p MTs in the touch receptor neurons (TRNs) MTs. Without MEC-17, MTs with between 11 and 15 protofilaments are seen. Loss of this enzymatic activity also changes the number and organization of the TRN MTs and affects TRN axonal morphology. In contrast, enzymatically inactive MEC-17 is sufficient for touch sensitivity and proper process outgrowth without correcting the MT defects. Thus, in addition to demonstrating that MEC-17 is required for MT structure and organization, our results suggest that the large number of 15-p MTs, normally found in the TRNs, is not essential for mechanosensation.
Conclusion:
These experiments reveal a specific role for α-TAT in the formation of MTs and in the production of higher order MTs arrays. In addition, our results indicate that the α-TAT protein has functions that require acetyltransferase activity (such as the determination of protofilament number) and others that do not (presence of internal MT structures).
Insights
The enzyme MEC-17 (α-tubulin acetyltransferase) produces 15-protofilament microtubules in touch neurons. While essential for microtubule structure, its enzymatic activity isn't required for touch sensation.
Area of Science:
- Cell Biology
- Neuroscience
- Cytoskeleton Dynamics
Background:
- Microtubules (MTs) are crucial cellular structures assembled from tubulin dimers.
- Most cells utilize 13-protofilament (13-p) MTs, but the mechanisms determining protofilament number remain unclear.
- Protofilament number may be influenced by the specific types of α- and β-tubulins present.
Purpose of the Study:
- To investigate the role of Caenorhabditis elegans α-tubulin acetyltransferase (α-TAT) MEC-17 in microtubule formation.
- To determine the necessity of MEC-17's enzymatic activity for microtubule structure and function in touch receptor neurons (TRNs).
Main Methods:
- Utilized genetic manipulation to study the effects of MEC-17 loss-of-function and enzymatic inactivation in C. elegans.
- Examined microtubule protofilament number, organization, and TRN axonal morphology.
- Assessed touch sensitivity and process outgrowth in relation to MEC-17 function.
Main Results:
- MEC-17's enzymatic activity is essential for producing 15-protofilament MTs in TRNs; without it, MTs with 11-15 protofilaments form.
- Loss of MEC-17 enzymatic activity alters TRN microtubule organization and axonal morphology.
- Enzymatically inactive MEC-17 supports touch sensitivity and axon outgrowth, indicating these functions are independent of its MT-structuring role.
Conclusions:
- α-TAT (MEC-17) plays a specific role in microtubule assembly and the formation of higher-order microtubule structures.
- MEC-17 possesses distinct functions: one dependent on its acetyltransferase activity (determining protofilament number) and others independent of it (e.g., maintaining internal MT structures).
- The abundance of 15-protofilament MTs in TRNs is not essential for mechanosensation.
More Related Videos
08:47Quantitative Approaches for Studying Cellular Structures and Organelle Morphology in Caenorhabditis elegans
Published on: July 5, 2019
07:21Quantitative Microtubule Fractionation Technique to Separate Stable Microtubules, Labile Microtubules, and Free Tubulin in Mouse Tissues
Published on: November 17, 2023
Related Concept Videos
Destabilization of Microtubules
Microtubule Instability
Microtubule Associated Motor Proteins
Assembly of Complex Microtubule Structures
Microtubule Associated Proteins (MAPs)
Microtubule Formation