The chemical class of Filamin 3 inhibitors is comprised of compounds that indirectly influence Filamin 3 function by targeting the actin cytoskeleton and associated cell signaling pathways. These inhibitors interact with various components of the cytoskeletal architecture and signaling mechanisms, impacting the role of Filamin 3 in cytoskeletal organization and cell signaling. Compounds such as Cytochalasin D, Latrunculin A, Jasplakinolide, and Swinholide A directly affect actin dynamics. Cytochalasin D and Latrunculin A inhibit actin polymerization, potentially disrupting the structural framework where Filamin 3 operates. Jasplakinolide and Phalloidin, on the other hand, stabilize actin filaments, which could alter Filamin 3's interactions with these structures. Swinholide A severs actin filaments, further influencing the actin network that Filamin 3 helps to organize and maintain.
In addition to actin-targeting compounds, inhibitors of kinases and proteins involved in actin cytoskeleton signaling pathways, such as Y-27632, ML-7, Blebbistatin, CCG-1423, and Wiskostatin, play a significant role. Y-27632 and CCG-1423 inhibit the RhoA/ROCK pathway, crucial for actin cytoskeleton rearrangement, potentially affecting Filamin 3's activity. ML-7 and Blebbistatin target myosin dynamics, influencing the contractile forces within the cytoskeleton, which can impact Filamin 3's role in cytoskeletal organization. SMIFH2 and CK-666, by inhibiting formin-mediated actin assembly and the Arp2/3 complex, respectively, affect actin filament formation and branching, further influencing the functional context of Filamin 3.
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