Arp23kompleksia

The Arp23kompleksia, also known as the Arp2/3 complex, is a crucial protein assembly involved in the regulation of actin filament formation in eukaryotic cells. This complex plays a vital role in the dynamic processes of the cytoskeleton, influencing cell shape, motility, and division. It is composed of seven subunits, with the Arp2 and Arp3 proteins forming the core structure.

The primary function of the Arp2/3 complex is to nucleate the growth of new actin filaments. It binds to the side of existing actin filaments and initiates the formation of a new filament branching off at a 70-degree angle. This branching mechanism is essential for generating the branched actin networks that are prevalent in cellular structures like lamellipodia, which are involved in cell crawling. The complex is activated by a family of proteins called the Wiskott-Aldrich syndrome verprolin-homologous (WAVE) proteins, which interact with the Arp2/3 complex and promote its nucleation activity.

In addition to its role in cell migration, the Arp2/3 complex is also implicated in other cellular processes such as endocytosis, the formation of filopodia, and the development of cellular protrusions. Its precise regulation is tightly controlled by various signaling pathways, ensuring that actin dynamics are adapted to the specific needs of the cell. Disruptions in Arp2/3 complex function can lead to a range of cellular defects and are associated with certain diseases.