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Cell surface (cortical) actin remodeling is a cyclic (9-step) process where each step is directly responsive to a cell signaling mechanism. Over the course of the cycle, actin begins as a monomer, elongates into a polymer with the help of attached actin-binding-proteins, and disassembles back into a monomer so the remodeling cycle may commence again.
The nucleation of new actin filaments – the rate-limiting step in actin polymerization – is aided by actin-nucleating proteins such as formins (like formin-2) and the Arp2/3 complex. [118] Formins help to nucleate long actin filaments. They bind two free actin-ATP molecules, bringing them together.
The oligomerization is the rate-determining step, considering actin filament formation as a whole. The so-called lag phase of actin polymerization originates from this step. It takes quite a while until polymerization starts, but once it has, the process is autocatalytic until the physiological maximum of the polymerization rate is reached.
The following steps describe one force-generating cycle of an actoclampin molecular motor: The polymerization cofactor profilin and the ATP·actin combine to form a profilin-ATP-actin complex that then binds to the end-tracking unit; The cofactor and monomer are transferred to the barbed-end of an actin already clamped filament
Actin plays a role in the formation of new spines as well as stabilizing spine volume increase. [1] The changes that actin brings about lead to the formation of new synapses as well as increased cell communication. Actin remodeling consists of the dynamic changes in actin polymerization that underlie the morphological changes at the neural synapse.
Actin polymerization can further be regulated by profilin and cofilin. [6] Cofilin functions by binding to ADP-actin on the negative end of the filament, destabilizing it, and inducing depolymerization. Profilin induces ATP binding to G-actin so that it can be incorporated onto the positive end of the filament.
This is a structure required to initiate the process of actin filament polymerization in a stable and efficient way. Nucleation factors such as WASP (Wiskott-Aldrich syndrome protein) help to form the seven-protein Arp2/3 nucleation complex , which resembles two actin monomers and therefore allows for easier formation of the polymerization nucleus.
Cytoskeletal drugs are small molecules that interact with actin or tubulin.These drugs can act on the cytoskeletal components within a cell in three main ways. Some cytoskeletal drugs stabilize a component of the cytoskeleton, such as taxol, which stabilizes microtubules, or Phalloidin, which stabilizes actin filaments.
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