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Actin and tubulin are the principal components of the cytoskeleton in eukaryotic cells, responsible for a wide array of essential cellular functions. - Actin exists as globular monomers (G-actin) that polymerize to form filamentous actin (F-actin) or microfilaments, which are involved in processes such as muscle contraction, movement, maintenance of cell shape, and intracellular transport[1][3][6][7]. Actin filaments are highly dynamic and interact with numerous binding partners to regulate their assembly and disassembly, controlled by the hydrolysis of ATP[1][2]. - Tubulin occurs as α- and β-tubulin heterodimers, which polymerize to form microtubules – hollow, stiff structures that provide tracks for intracellular transport, participate in chromosome segregation during mitosis, and help determine overall cell shape and polarity[2][6][7]. The dynamics of microtubule growth and shrinkage are regulated through GTP binding and hydrolysis[2]. - Together, actin and tubulin form integrated networks that allow cells to adapt their structure in response to internal and external signals, drive critical processes such as cytokinesis and cell migration, and maintain mechanical integrity[3][4][5][6][7]. - Both protein families are validated targets for several anticancer and antifungal drugs that disrupt filament dynamics, but their ubiquitous cellular roles make toxicity a challenge[4][5]. Note: This entity, "Actin and Tubulin," is a grouping of two distinct protein classes, not a single canonical molecular target. For structured drug databases, information should ideally be split into "Actin (ACTA1, ACTB, etc.)" and "Tubulin (TUBA1A, TUBB, etc.)," as each family comprises multiple gene products with separate drug interactions, disease associations, and molecular mechanisms[2][6][7].
Stabilization of microtubules, Inhibition of microtubule polymerization, Inhibition of actin polymerization, Stabilization of actin filaments
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