WAVE homology in membrane protrusions (Wmp) activators consist of compounds that influence the actin cytoskeleton and related signaling pathways, leading to enhanced functional activity of Wmp. Compounds such as Jasplakinolide and Phalloidin directly bind to actin, promoting filament stabilization, which can indirectly enhance Wmp activity as it operates in conjunction with the Arp2/3 complex to facilitate actin polymerization. Stabilization of actin filaments by these compounds can create a cellular environment that necessitates the involvement of Wmp to extend or create new filaments, thereby enhancing its functional role in actin dynamics.
Other chemicals, like CK-666 and Cytochalasin D, disrupt normal actin polymerization through various mechanisms, leading to cellular compensatory responses that can include the upregulation of Wmp activity. In response to actin dynamics disruption, Wmp may be activated to restore or maintain cellular structures such as membrane protrusions and cell motility. Compounds such as Y-27632 and Blebbistatin interfere with actomyosin contractility, which could lead to increased reliance on Wmp to promote actin polymerization in the context of altered cellular mechanics. Furthermore, inhibitors of small GTPases like NSC 23766 and ML141 may indirectly enhance Wmp activity by affecting upstream regulators of actin polymerization, creating a feedback loop that drives the activity of Wmp as the cell seeks to compensate for the inhibited signaling.
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