Role of Formins in Actin Assembly: Nucleation and Barbed-End Association

By David Pruyne, M. Evangelista, Changsong Yang, E. Bi, S. Zigmond, A. Bretscher, Charles Boone. Science, 2002

806 citations recorded by the source corpus.

Subfields: Cardiology and Cardiovascular Medicine, Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/18067c346249d648e6ddbdb1072b65c9528da2d5

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cardiology and Cardiovascular Medicine

T. Svitkina

In Cell Biology

In Molecular Biology

Citations in the corpus

Conserved microtubule–actin interactions in cell movement and morphogenesis (2003, background): “7 ), and the formin, mDia, which regulates actin polymerization into bundle”
Cell migration: Rho GTPases lead the way. (2004, background): “…target of Rho is mDia, the mammalian ortholog of Drosophila Diaphanous. mDia belongs to the formin-homology containing family of proteins, which have been linked to actin filament assembly in both Drosophila and yeast (Castrillon and Wasserman, 1994; Pruyne et al., 2002; Sagot et al., 2002).”
Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. (2004, methodology): “The FH2 domain is sufficient for actin nucleation in vitro, while the FH1 domain is required for in vivo2 Department of Cell Biology Harvard Medical School function and binds profilin (Sagot et al., 2002b; Pruyne et al., 2002; Pring et al., 2003).”
Adhesion-dependent cell mechanosensitivity. (2003, background): “Recent studies demonstrated that the yeast homolog of Dia1, known as Bni1p, is a potent nucleator of actin polymerization (Pruyne et al. 2002, Sagot et al. 2002).”
How and why does β‐actin mRNA target? (2005, background): “Diaphanous (Castrillon and Wasserman, 1994) is required for cytokinesis, Bni1p is concentrated at the tips of mating projections and can nucleate actin polymerization in vitro (Pruyne et al., 2002; Sagot et al., 2002) and is required for yeast bud formation (Evangelista et al.”
Cell Wall Integrity Signaling in Saccharomyces cerevisiae (2005, background): “A second domain that is highly conserved among family members, called FH2, nucleates actin polymerization in vitro (263, 285, 286).”
Regulation of actin assembly associated with protrusion and adhesion in cell migration. (2008, background): “In addition to its nucleating activity, the FH2 domain binds to the barbed end and acts as a “leaky capper” by slowing down the elongation and dissociation rates (170, 171, 266) without affecting the critical concentration.”
The role of the Rho GTPases in neuronal development. (2005, background): “…(Pring et al. 2003; Zigmond et al. 2003), and they enhance actinnucleation via their Formin homology FH1-FH2 or FH2 domains (Tominaga et al. 2000; Copeland and Treisman 2002; Pruyne et al. 2002; Sagot et al. 2002; Kovar et al. 2003; Li and Higgs 2003; Pring et al. 2003; Shimada et al. 2004).”
Regulation of Cell Wall Biogenesis in Saccharomyces cerevisiae: The Cell Wall Integrity Signaling Pathway (2011, background): “Bni1 and Bnr1 nucleate actin filament assembly and protect actin filaments from capping protein (Fujiwara et al. 1998; OzakiKuroda et al. 2001; Pruyne et al. 2002; Sagot et al. 2002a,b; Evangelista et al. 2003).”
Mechanism of filopodia initiation by reorganization of a dendritic network (2003, background): “For example, proteins of the formin family have recently been shown to nucleate actin filaments in vitro (Pruyne et al., 2002; Sagot et al., 2002b) and induce actin cables in yeast in vivo in the absence of the Arp2/3 complex (Evangelista et al., 2002; Sagot et al., 2002a).”
Genetic and cell biological analysis of integrin outside-in signaling. (2009, background): “Here actin assembly is mediated by the diaphanous-related formin (DRF) protein family, which was shown to be essential for organization and dynamics of lamellar F-actin as well as for the turnover of FAs (Pruyne et al. 2002).”