Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation
Bruno Carmona1,2, H Susana Marinho3, Catarina Lopes Matos1
1Centro de Química Estrutural, Institute of Molecular Sciences, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal.
Biology
|April 28, 2023
Summary
Tubulin acetylation, a key post-translational modification, impacts microtubule stability and flexibility. This review explores its roles in cell biology, stress response, and human pathologies.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Microtubules (MTs) are essential eukaryotic polymers involved in diverse cellular processes.
- Post-translational modifications (PTMs) of tubulin, such as acetylation, diversify MT functions.
- Tubulin acetylation's precise roles remain under investigation.
Purpose of the Study:
- To review the current understanding of tubulin acetylation.
- To discuss the regulation and cellular impacts of tubulin acetylation.
- To explore the link between MT acetylation and disease.
Main Methods:
- Literature review of experimental data on tubulin acetylation.
- Analysis of studies on tubulin acetyltransferases and desacetylases.
- Examination of MT acetylation in stress responses and pathologies.
Main Results:
- Lys40 acetylation of α-tubulin is linked to MT stabilization and flexibility.
- Acetylation alters MT mechanical properties, preventing damage.
- Changes in MT acetylation are observed under stress and in diseases.
Conclusions:
- Tubulin acetylation is a crucial regulator of microtubule dynamics and mechanics.
- Dysregulation of tubulin acetylation impacts cell physiology and disease states.
- Further research is needed to fully elucidate the roles of tubulin acetylation.
Keywords:
HDAC6Lys40SIRT2acetylationmicrotubule-associated proteinsmicrotubule-mechanical propertiesmicrotubulespost-translational modificationstubulinαTAT1More Related Videos
Related Concept Videos
Covalently Linked Protein Regulators
6.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.9K
Phase II Reactions: Acetylation Reactions
285
Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
285
Histone Modification
13.4K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
13.4K
Assembly of Complex Microtubule Structures
1.9K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
1.9K
Spreading of Chromatin Modifications
8.3K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
Writers
The writer...
8.3K
Transfer RNA Synthesis
12.1K
One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
12.1K


