A Nucleator Arms Race: Cellular Control of Actin Assembly

By Kenneth G. Campellone, Matthew Welch. Nature reviews. Molecular cell biology, 2010

948 citations recorded by the source corpus.

For over a decade, the actin-related protein 2/3 (ARP2/3) complex, a handful of nucleation-promoting factors and formins were the only molecules known to directly nucleate actin filament formation de novo. However, the past several years have seen a surge in the discovery of mammalian proteins with roles in actin nucleation and dynamics. Newly recognized nucleation-promoting factors, such as WASP and SCAR homologue (WASH), WASP homologue associated with actin, membranes and microtubules (WHAMM), and junction-mediating regulatory protein (JMY), stimulate ARP2/3 activity at distinct cellular locations. Formin nucleators with additional biochemical and cellular activities have also been uncovered. Finally, the Spire, cordon-bleu and leiomodin nucleators have revealed new ways of overcoming the kinetic barriers to actin polymerization.

Subfields: Biomedical Engineering, Cell Biology

View Paper: https://www.semanticscholar.org/paper/fc17aeaf93fccec12a56b63ec3126429fdfec1a4

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Citations in the corpus

• Life at the leading edge. (2011, background): “One of these proteins, CordonBleu, is localized in lamellipodia and, when overexpressed, it increases the number of cells with lamellipodia and membrane ruffles (Campellone and Welch, 2010).”
• Actin dynamics, architecture, and mechanics in cell motility. (2014, background): “Numerous polymerization nucleation factors play a role in lamellipodia formation, but the main mode of filament assembly is via the Arp2/3 complex activated by a specific NPF, the WAVE complex, although formins may also play a role (48).”
• Actin and Actin-Binding Proteins. (2016, background): “A similar protein complex regulates WASH (Campellone and Welch 2010).”
• Regulation of Cell Wall Biogenesis in Saccharomyces cerevisiae: The Cell Wall Integrity Signaling Pathway (2011, background): “Of key importance is the association of the actin-binding protein profilin (Pfy1), which enhances filament formation by delivery of actin to the formin at the plasma membrane (Sagot et al. 2002b; Pring et al. 2003; for a recent review, also see Campellone and Welch 2010).”
• Rac and Rho GTPases in cancer cell motility control (2010, background): “Rac stimulates new actin polymerization, acting on Arp2/3 complex, which binds to a family of proteins called nucleating promoting factors (for detailed description of actin nucleation factors refer to [29,30]) and initiates the formation of new actin filaments on the sides of existing filaments to ”