Microtubule Targeting Agents in Disease: Classic Drugs, Novel Roles
Abstract
:Simple Summary
Abstract
1. Microtubules and Tubulin
2. Microtubule-Targeting Agents (MTAs)
- −
- Vinca domain (MDA, orange in Figure 2): this domain is located in the β tubulin monomer at the inter-dimer interface between two longitudinally aligned tubulin dimers. Drugs that bind to this domain inhibit the assembly of tubulin by sequestering tubulin into paracrystalline aggregates. Examples of these drugs are vincristine, vinblastine, and vindesine [12,13,14,15].
- −
- Colchicine site (MDA, cyan in Figure 2): this site is in the β tubulin monomer in a deep pocket space between the αβ-tubulin dimer itself. Binding to this site inhibits microtubule formation by preventing a conformational change in tubulin required for polymerization. Colchicine, benzimidazoles (e.g., nocodazole), and combretastatins are among the drugs that bind to this site [16,17].
- −
- Taxane site (MSA, red in Figure 2): it is located at the β tubulin monomer in the lumen of microtubules. Binding to this site stabilizes the MT lattice. Interestingly, MT-stabilizing drugs, such as paclitaxel and epothilone, achieve their microtubule-stabilizing effect through pharmacologically distinct mechanisms despite binding competitively to the same taxane site [18].
- −
- −
- Laulimalide/peloruside site (MSA, magenta in Figure 2): this site is located in a pocket of the β-tubulin that faces the outside of the MT. Studies suggest that they inhibit microtubule disassembly by acting as molecular ‘clamps’ that hold together protofilaments. The drugs Laulimalide and Peloruside isolated from marine sponges gave name to this group [22,23,24].
- −
- −
- Gatorbulin site (MDA, yellow in Figure 2): this new site has been described in 2021, is located in the α-tubulin subunit (between α- and β-tubulin) close to the colchicine site, and it functions in a similar way to the vinca site, creating a wedge between two longitudinally aligned tubulin dimers at the end of MTs [10]. Recently, a new compound called Cevipabulin has been described to also bind to this pocket [11].
3. MTAs and Pathogens
4. MTAs and Neurodegenerative Diseases
Tauopathies
5. MTAs and Cancer
5.1. How Can MTAs Kill Cancer Cells through Mitosis-Independent Mechanisms?
5.2. MTAs and Intracellular Trafficking
5.3. MTAs and Cell Death by Apoptosis
5.4. MTAs and Effects on the Tumor Vascular Tissue
5.4.1. Antiangiogenic Effects
5.4.2. Vasculature-Disrupting Effects
5.5. MTAs, Metastasis, and Cell Migration
6. MTAs and Drug Resistance
7. Conclusions
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
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Wordeman, L.; Vicente, J.J. Microtubule Targeting Agents in Disease: Classic Drugs, Novel Roles. Cancers 2021, 13, 5650. https://doi.org/10.3390/cancers13225650
Wordeman L, Vicente JJ. Microtubule Targeting Agents in Disease: Classic Drugs, Novel Roles. Cancers. 2021; 13(22):5650. https://doi.org/10.3390/cancers13225650
Chicago/Turabian StyleWordeman, Linda, and Juan Jesus Vicente. 2021. "Microtubule Targeting Agents in Disease: Classic Drugs, Novel Roles" Cancers 13, no. 22: 5650. https://doi.org/10.3390/cancers13225650