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As an integral component of the mammalian cell cytoskeleton, actin is involved in multiple physiological functions, including cell growth, motility, trafficking, and division. These basic functions require remodeling of the actin cytoskeleton, as well as extension and withdrawal of actin-based cellular neurites (e.g., lamellipodia, filopodia), all of which rely upon rapid dynamic cycling between filamentous actin (F-actin) and monomer actin (G-actin)1. Correspondingly, dysfunctional actin cytoskeletal dynamics are a pathophysiological feature of many human diseases, with perhaps cancer being the prototypical example. For these reasons, actin is a theoretically attractive anti-cancer therapeutic target. However, in practice, actin has proven to be a poor target because of toxic side effects due in large part to the inability of therapeutics to distinguish between actin isoforms.2,3,. Thus, the actin in cancerous and healthy cells are affected by cancer therapies acting directly upon actin, leading to toxic side effects in different organ systems (e.g., heart and diaphragm)2,3. Recently, drug discovery has shifted from actin to actin-associated structural proteins such as the Arp2/3 complex and tropomyosins (Tpms) as these proteins offer multiple isoforms for selective targeting and the opportunity to avoid toxic side effects2-4 (Fig. A).

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 Also included in this newsletter:

  • Tubulin and Actin Live Cell Reagents, G-LISA Activation Assay Kits, Tubulin Kits, Actin Biochem Kits
  • Related Publications

 

    Posted in News By

    Ryan Kogstad