Search results
Results from the WOW.Com Content Network
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.
Many actin-related molecules create a free barbed end for polymerization by uncapping or severing pre-existing filaments and using these as actin nucleation cores. However, the Arp2/3 complex stimulates actin polymerization by creating a new nucleation core. Actin nucleation is an initial step in the formation of an actin 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.
(Single white dots represent monomers and black chains represent oligomers and polymers) [1] Comparison of molecular weight vs conversion plot between step-growth and living chain-growth polymerization. In polymer chemistry, step-growth polymerization refers to a type of polymerization mechanism in which bi-functional or multifunctional ...
Association of G-actin into F-actin is regulated by the critical concentration outlined below. 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.
The unfavorable kinetics of actin oligomer production prevent spontaneous actin polymerization. [2] Once an actin nucleus has been created, the connection of the monomers happens swiftly, with the plus end developing considerably more quickly than the minus end. [2] Actin's ATPase activity sharply rises after insertion into the filament. [2]
Akt phosphorylates many proteins involved in polymerisation and stabilisation of the actin cytoskeleton. In normal cells, this can either increase the stability of cytoskeleton components or promote migration via remodelling. Examples are listed below: Actin filaments - Akt phosphorylates actin directly [36]
In contrast to Listeria, the actin filaments are organized in long, unbranched parallel bundles. The Arp2/3 complex is only localized near the bacterial surface and thus it is assumed that a more frequent Arp2/3 complex-independent elongation occurs. [16] In Burkholderia pseudomallei BimA initiates actin polymerization in vitro. It is assumed ...