TABLE 1.
Name | Target | Function |
Small molecules | ||
Tetracyclines* | Actin | Reduces overall size of the complete actin aggregate (Pathak et al., 2021). |
Miuraenamide* | Actin | Binds to actin monomers by manipulating the DNase-1 binding which aids polymerization; prevents cofilin binding (Wang et al., 2021). |
Pyrollopyridines† | LIMK | Inhibits LIMK through its ATP binding site, inhibiting cofilin phosphorylation (Ariawan et al., 2021). |
Deubiquitinase Inhibitors† | Deubiquitinase | Promote F-actin assembly independently of other pathways or through cofilin dephosphorylation (Larbret et al., 2022). |
Cucurbitacin-B* | VASP | Inactivates VASP by phosphorylation and prevents actin remodeling, resulting in actin aggregation (Zhang et al., 2014). |
Pyr1† | LIMK | Inhibits LIMK, leading to increased cofilin activation and actin dynamics (Gory-Fauré et al., 2021). |
NOX Inhibitors* | NOX | Various (Vas2870, et al) inhibitors of NOX prevent ROS production (Barua et al., 2019). |
Peptides | ||
Cofilin-derived peptides* | Cofilin, LIMK, or SSH1 | Regulates different targets in the actin-cofilin pathway depending on the design of the peptide (Shaw and Bamburg, 2017). |
Proteins | ||
SGK1† | Ion channels, Na+/K+-ATPase | Up-regulates the activity and expression of many ion channels and Na+/K+-ATPase (Lang et al., 2010). |
Hsp70† | Unfolded or misfolded proteins | Assists in folding of new proteins, proofreading and refolding of misfolded proteins, and translocation of proteins to organelles (Mayer and Bukau, 2005). |
LIMK* | Cofilin | Phosphorylates and inactivates cofilin (Zhang et al., 2021a). |
*A direct link has been found to cofilin-actin rods.
†Hypothesized link to cofilin-actin rods.