karyopherin β2 Inhibitors

Karyopherin β2 inhibitors represent a diverse array of compounds strategically designed to modulate the cellular functions governed by the nuclear transport protein. Importazole, for instance, selectively inhibits importin-β, disrupting nuclear import processes and potentially impacting karyopherin β2-mediated shuttling. Additionally, CRM1 inhibitors like KPT-330, NSC 281668, and Leptomycin B hinder nuclear export, indirectly affecting karyopherin β2-mediated transport by disrupting exportin-dependent pathways. The compound Ivermectin, known for its antiparasitic properties, exhibits an unexpected role in altering importin-α/β-mediated nuclear import, providing potential avenues for modulating karyopherin β2-related cellular processes. Nucleozin selectively inhibits importin-β, potentially influencing karyopherin β2-mediated nuclear import by disrupting the importin-β pathway.

Furthermore, small molecules like MLN4924 and CKI-7 target key cellular pathways, including the NEDDylation pathway and Casein kinase I, respectively. MLN4924 inhibits NEDD8-activating enzyme, leading to indirect effects on karyopherin β2 through alterations in post-translational modifications. CKI-7, a Casein kinase I inhibitor, influences phosphorylation events, potentially modulating karyopherin β2 by altering its post-translational modifications and cellular localization dynamics. SINE compounds, such as KPT-185, KPT-251, and KPT-276, selectively inhibit XPO1 (Exportin-1), disrupting nuclear export and potentially influencing karyopherin β2-related processes through disruptions in exportin-dependent pathways. Dibenzazepine (DBZ), a gamma-secretase inhibitor, indirectly impacts karyopherin β2 by altering Notch signaling, associated with nuclear transport regulation and potential impacts on karyopherin β2-mediated processes. Collectively, these inhibitors offer a comprehensive toolkit for dissecting and manipulating the intricate regulatory networks governed by karyopherin β2 in cellular transport processes.