Cellular Motility Driven by Assembly and Disassembly of Actin Filaments
@article{Pollard2003CellularMD, title={Cellular Motility Driven by Assembly and Disassembly of Actin Filaments}, author={Thomas D. Pollard and Gary G. Borisy}, journal={Cell}, year={2003}, volume={112}, pages={453-465}, url={https://api.semanticscholar.org/CorpusID:6887118} }
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Biology
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Biology
Three functions of this surface-associated actin monomer pool are described, including regulating network density via product inhibition of the Arp2/3 complex, accelerating filament elongation as a distributive polymerase, and converting profilin-actin into a substrate for the ArP2/ 3 complex.
Load fluctuations drive actin network growth
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Biology, Physics
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Biology, Physics
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Biology
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Biology
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Biology
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Biology
A complex of seven proteins called Arp2/3 complex is the best characterized cellular initiator of actin filament nucleation, and its interactions provide a final common pathway for many signaling inputs to regulate actin polymerization.
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Biology
Branching occurs during, rather than after, nucleation by Arp2/3 complex activated by the Wiskott–Aldrich syndrome protein (WASP or Scar protein), which results in the automatic assembly of the branched actin network after activation by proteins of the WASP/Scar family and favour the selective disassembly of proximal regions of the network.
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Biology
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Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin.
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Biology, Chemistry
This work re-examined the hydrolysis of ATP by polymerized actin using mechanical quenched-flow methods to improve temporal resolution and expects that profilin will block subunit addition at the barbed end of a filament.