NEURL1B Inhibitors

NEURL1B, or neuralized E3 ubiquitin protein ligase 1B, plays a crucial role in ubiquitin-dependent endocytosis, particularly within the actin cytoskeleton and cytosol. This protein is predicted to enable ubiquitin protein ligase activity, emphasizing its significance in cellular processes. To explore potential inhibitors, we considered indirect approaches targeting specific signaling pathways associated with NEURL1B. Several chemicals were identified for their ability to influence NEURL1B indirectly. For instance, PMA, a phorbol ester, activates protein kinase C (PKC), impacting NEURL1B by modulating PKC-mediated signaling, ultimately altering the ubiquitin-dependent endocytosis pathway. Chloroquine, a lysosomotropic agent, disrupts endocytosis by impairing lysosomal function, thereby indirectly inhibiting NEURL1B within the actin cytoskeleton and cytosol.

Other inhibitors, such as Brefeldin A and Wortmannin, disrupt vesicular transport and the PI3K/AKT signaling pathway, respectively, indirectly affecting NEURL1B. These alterations influence the ubiquitin-dependent endocytosis pathway and NEURL1B's function within the actin cytoskeleton. Similarly, compounds like Latrunculin B, Dynasore, and 2-Deoxyglucose impact NEURL1B by disrupting the actin cytoskeleton, endocytosis, and cellular energy metabolism, respectively. Furthermore, chemicals like Tunicamycin interfere with protein glycosylation, affecting NEURL1B indirectly by disrupting proper protein folding and trafficking. U0126, GW5074, and LY294002, targeting the MAPK and PI3K/AKT pathways, indirectly modulate NEURL1B by altering SPRY4 expression and function. In summary, understanding NEURL1B's involvement in ubiquitin-dependent endocytosis and its localization within the actin cytoskeleton provides valuable insights for identifying potential inhibitors. The presented chemicals, through their distinct mechanisms, showcase the intricate interplay of cellular pathways influencing NEURL1B and offer avenues for further exploration in the context of cellular regulation and function.