Global treadmilling coordinates actin turnover and controls the size of actin networks
MF Carlier, S Shekhar - Nature Reviews Molecular Cell Biology, 2017 - nature.com
Various cellular processes (including cell motility) are driven by the regulated, polarized
assembly of actin filaments into distinct force-producing arrays of defined size and …
assembly of actin filaments into distinct force-producing arrays of defined size and …
Actin‐depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics
M Poukkula, E Kremneva, M Serlachius… - …, 2011 - Wiley Online Library
Actin filaments form contractile and protrusive structures that play central roles in many
processes such as cell migration, morphogenesis, endocytosis, and cytokinesis. During …
processes such as cell migration, morphogenesis, endocytosis, and cytokinesis. During …
Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament
Intracellular and extracellular mechanical forces affect the structure and dynamics of the
actin cytoskeleton. However, the underlying molecular and biophysical mechanisms …
actin cytoskeleton. However, the underlying molecular and biophysical mechanisms …
Cofilactin filaments regulate filopodial structure and dynamics in neuronal growth cones
RK Hylton, JE Heebner, MA Grillo… - Nature communications, 2022 - nature.com
Cofilin is best known for its ability to sever actin filaments and facilitate cytoskeletal recycling
inside of cells, but at higher concentrations in vitro, cofilin stabilizes a more flexible, hyper …
inside of cells, but at higher concentrations in vitro, cofilin stabilizes a more flexible, hyper …
Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries
Actin-based motility demands the spatial and temporal coordination of numerous regulatory
actin-binding proteins (ABPs)[1], many of which bind with affinities that depend on the …
actin-binding proteins (ABPs)[1], many of which bind with affinities that depend on the …
Cofilin-linked changes in actin filament flexibility promote severing
The actin regulatory protein, cofilin, increases the bending and twisting elasticity of actin
filaments and severs them. It has been proposed that filaments partially decorated with …
filaments and severs them. It has been proposed that filaments partially decorated with …
Torsional stress generated by ADF/cofilin on cross-linked actin filaments boosts their severing
Proteins of the actin depolymerizing factor (ADF)/cofilin family are the central regulators of
actin filament disassembly. A key function of ADF/cofilin is to sever actin filaments. However …
actin filament disassembly. A key function of ADF/cofilin is to sever actin filaments. However …
Cellular force‐sensing through actin filaments
The actin cytoskeleton orchestrates cell mechanics and facilitates the physical integration of
cells into tissues, while tissue‐scale forces and extracellular rigidity in turn govern cell …
cells into tissues, while tissue‐scale forces and extracellular rigidity in turn govern cell …
Utilizing machine learning to greatly expand the range and accuracy of bottom-up coarse-grained models through virtual particles
PG Sahrmann, TD Loose… - Journal of Chemical …, 2023 - ACS Publications
Coarse-grained (CG) models parametrized using atomistic reference data, ie,“bottom up”
CG models, have proven useful in the study of biomolecules and other soft matter. However …
CG models, have proven useful in the study of biomolecules and other soft matter. However …
Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments
AR Huehn, JP Bibeau, AC Schramm… - Proceedings of the …, 2020 - National Acad Sciences
Members of the cofilin/ADF family of proteins sever actin filaments, increasing the number of
filament ends available for polymerization or depolymerization. Cofilin binds actin filaments …
filament ends available for polymerization or depolymerization. Cofilin binds actin filaments …