CLASP (Cytoplasmic Linker Associated Protein) Inibitori

CLASP (Cytoplasmic Linker Associated Protein) is a key regulatory protein involved in microtubule dynamics and cellular processes such as mitosis and cell migration. It primarily functions to stabilize microtubules by binding to their plus-ends, thereby preventing depolymerization and promoting microtubule growth. CLASP is also known to interact with various other cellular proteins, including kinases and motor proteins, thereby serving as a scaffold that integrates multiple signaling pathways. For example, phosphorylation events mediated by proteins like Polo-like kinase 1 (Plk1) and Glycogen Synthase Kinase 3 (GSK3) can regulate CLASP activity and its interaction with microtubules. The coordinated activity of CLASP and its interacting partners plays a critical role in cellular processes requiring dynamic microtubule behavior, such as during the cell cycle and cellular migration.

CLASP (Cytoplasmic Linker Associated Protein) Inhibitors are a category of small molecules designed to modulate the activity of CLASP proteins. These proteins play a critical role in microtubule dynamics, affecting cellular processes such as cell division and migration. Inhibition of CLASP is primarily aimed at disrupting its stabilizing effect on microtubules, which in turn can influence a wide array of intracellular activities. CLASP Inhibitors can target the protein either directly by binding to specific domains involved in microtubule interaction or indirectly by modulating the activities of kinases and other proteins that post-translationally modify CLASP.