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The dynamic nature of actin polymerization and disassembly is central to functions such as cell adhesion and migration. For this reason, molecular mechanisms of actin reorganization are under investigation for therapeutics targeting cancer and cardiovascular diseases.
We have highlighted some key actin nucleators, regulatory proteins, and toxins that can help you study the actin polymerization process at different stages.
Nucleation and elongation factors that promote linear actin filaments
ARP 2/3 complex
Mimics actin trimer and acts as a nucleation site to form branched actin filaments (see Figure 1)
Regulator of the Arp2/3 complex
Organizes up actin monomers into a prenucleation scaffold for polymerization
G-actin-sequestering protein which allows filament polymerization
Facilitates the formation of ATP-actin monomers, which are then available for polymerization
Increases dissociation of actin monomers from filaments causing depolymerization
Binds tightly to actin filaments and prevents their dissociation (depolymerization inhibitor)
Binds to actin monomers to inhibit polymerization - promotes filament disassembly
Binds to the plus ends of actin filaments and prevent filament assembly and disassembly
Stabilizes actin monomers and induces actin polymerization
Inhibits actin polymerization
Figure 1. CytoPainter F-actin Staining Kit - Blue Fluorescence (ab112124). F-actin was stained with CytoPainter blue in mouse embryonic stem cell-differentiated embryoid bodies using ICC/IF. Image courtesy of Dr. Shaohua Li, UMDNJ-Robert Wood Johnson Medical School.