β2C Tubulin is a fundamental structural component of microtubules, which are cylindrical polymers composed of tubulin dimers, playing a critical role in numerous cellular processes including mitosis, cell motility, and intracellular trafficking. This specific isoform of tubulin is integral in the heterodimer formation with α-tubulin, facilitating the dynamic assembly and disassembly of microtubules. The precise regulation of microtubule dynamics is essential for the proper functioning of cells, with β2C tubulin being pivotal in maintaining this balance. Its expression and activity are tightly controlled, reflecting its importance in cellular architecture and signaling pathways. As a critical player in the cytoskeleton's structure and function, alterations in β2C tubulin expression or function can profoundly affect cell division, differentiation, and migration, underlying its significance in cellular physiology.
The inhibition of β2C tubulin impacts cellular functions by disrupting microtubule dynamics, which is essential for many aspects of cell activity including mitosis. Inhibitors affect the polymerization and depolymerization processes of microtubules, either by stabilizing them in a polymerized state or by preventing their assembly, leading to a blockade of microtubule dynamics. This disruption can lead to the inhibition of cell division, as the mitotic spindle, which is crucial for segregating chromosomes to daughter cells, cannot form properly without functional microtubules. Additionally, the inhibition of β2C tubulin can affect cell motility and signal transduction pathways that are reliant on the structural integrity and dynamic functions of the microtubule network. By targeting the critical balance of microtubule assembly and disassembly, inhibitors can thus exert profound effects on cell viability and function, highlighting the complex interplay between microtubule dynamics and cellular processes. The precise mechanism of action of such inhibitors involves direct binding to the tubulin monomers or influencing the regulatory proteins involved in microtubule dynamics, showcasing the intricate nature of targeting β2C tubulin for inhibiting its function within the cell.
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