Tubulin and microtubule-associated proteins (MAPs) (Tubulin/MAPs)

Tubulin and microtubule-associated proteins (MAPs) constitute the primary structural components of the cellular cytoskeleton, essential for maintaining cell architecture, facilitating intracellular transport, and orchestrating chromosome segregation during mitosis [1, 2]. Tubulin exists as alpha and beta heterodimers that polymerize into dynamic microtubules, while MAPs regulate their stability, assembly, and interaction with other cellular components [2]. The nuclear matrix serves as a proteinaceous scaffold within the nucleus, providing structural support for chromatin organization and DNA-related processes [3]. In clinical oncology, tubulin is a cornerstone therapeutic target; microtubule-targeting agents (MTAs) such as taxanes and vinca alkaloids disrupt spindle dynamics, leading to cell cycle arrest at the metaphase-anaphase transition and subsequent apoptosis [4]. Beyond cancer, MAPs like Tau are critical targets in neurodegenerative research due to their role in stabilizing axonal microtubules and their pathological aggregation in tauopathies [5]. The nuclear matrix also contains proteins involved in genomic stability that are targeted by specific chemotherapeutic agents to disrupt cancer cell proliferation [3].

Other names

MicrotubulesAlpha-tubulinBeta-tubulinNuclear matrix proteinsTubulin and microtubule-associated proteins; nuclear matrix

Microtubule-targeting agents (MTAs) act by binding to specific sites on tubulin dimers to either stabilize microtubules against depolymerization (e.g., taxanes, epothilones) or inhibit their polymerization (e.g., vinca alkaloids, eribulin), both of which disrupt the mitotic spindle and trigger cell cycle arrest and apoptosis [4, 5].