Cellular motility driven by assembly and disassembly of actin filaments.

By Thomas D. Pollard, Gary G. Borisy. Cell, 2003

2,526 citations recorded by the source corpus.

Subfields: Biomedical Engineering, Cell Biology

View Paper: https://www.semanticscholar.org/paper/ede4e92349166c27b80863740efe8a3dd26d9d44

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In Biomedical Engineering

In Cell Biology

Citations in the corpus

Actin Structure and Function (2011, neutral): “Numerous ABPs are involved in the regulation of actin cytoskeleton dynamics (44).”
Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective (2012, background): “The actin-based protrusions of eukaryotic cells [1006, 1007, 1008, 1009, 1010, 1011, 1012, 1013, 1014, 1015, 1016, 1017, 1018, 1019, 1020, 1021, 1022].”
The biophysics of neuronal growth (2010, background): “When bent away from the cell surface, a G-actin subunit can ‘squeeze’ in, lengthening the filaments; when straightening against the surface, the restoring force of the filament delivers a propulsive force, thus pushing the filopodial and lamellipodial edge forward [83].”
Cell mechanics and the cytoskeleton (2010, neutral): “This steady elongation is well suited to producing the sustained forces that are required to advance the leading edge of a migrating cel”
Actin in dendritic spines: connecting dynamics to function (2010, background): “An elegant study by the Svitkina laboratory investigated the cytoskeletal organization of dendritic JCB • VOLUME 189 • NUMBER 4 • 2010 622 pool by restricting the polymerization only to the areas where it is required (Pollard and Borisy, 2003).”
The physics of cancer: the role of physical interactions and mechanical forces in metastasis (2011, neutral): “Much of what we have learned about the physical and molecular mechanisms driving normal and cancer cell motility has come from in vitro studies using two-dimensional (2D) substrate”
Adhesion-dependent cell mechanosensitivity. (2003, background): “Both filament polymerization and branching depend on a molecular complex known as Arp2/3, which nucleates filament growth and mediates their attachment to preexisting filaments (Borisy & Svitkina 2000, Pollard & Borisy 2003).”
α-Catenin Is a Molecular Switch that Binds E-Cadherin-β-Catenin and Regulates Actin-Filament Assembly (2005, neutral): “Therefore, we examined whether α-catenin can influence Arp2/3 complexmediated actin assembly, which plays a central role in actin assembly and branching in lamellipodia (Pollard and Borisy, 2003) and is localized to sites of initiating cell-cell contact (Kovacs et al., 2002).”
Actin dynamics, architecture, and mechanics in cell motility. (2014, background): “One of the main mechanisms for remodeling actin networks is to disassemble them as an ensemble, a concept referred to in the cellular context as the “treadmilling array” model (245).”
Lipid raft microdomains and neurotransmitter signalling (2007, background): “Phosphoinositide lipids such as PtdIns(4,5)P 2 and PtdIns(3,4)P 2 have been shown to accumulate in lipid rafts, and these lipids are also known to bind actin and direct actin assembly into filament”
The WASP–WAVE protein network: connecting the membrane to the cytoskeleton (2007, background): “The VCA region binds to an actin monomer and to the ARP2/3 complex , leading to a burst of actin polymerization through the activation of the ARP2/3 complex, which mediates nucleation of actin polymerizatio”
Life at the leading edge. (2011, background): “Since the ‘‘textbook’’ model for actin dynamics in lamellipodia was first described by Pollard and Borisy (2003), our understanding of how protrusions are initiated, extended, and retracted has increased on numerous fronts.”