Abstract
The most important discovery in the field is that the Arp2/3 complex nucleates assembly of actin filaments with free barbed ends. Arp2/3 also binds the sides of actin filaments to create a branched network. Arp2/3's nucleation activity is stimulated by WASP family proteins, some of which mediate signaling from small G-proteins. Listeria movement caused by actin polymerization can be reconstituted in vitro using purified proteins: Arp2/3 complex, capping protein, actin depolymerizing factor/cofilin, and actin. actin depolymerizing factor/cofilin increases the rate at which actin subunits leave pointed ends, and capping protein caps barbed ends.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Actin Cytoskeleton / chemistry
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Actin Cytoskeleton / metabolism*
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Actin Depolymerizing Factors
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Actin-Related Protein 2
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Actin-Related Protein 3
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Actins / metabolism*
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Animals
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CapZ Actin Capping Protein
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Carrier Proteins / metabolism
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Cell Movement
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Cytoskeletal Proteins*
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Gelsolin / metabolism
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Humans
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Microfilament Proteins / metabolism
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Molecular Motor Proteins / metabolism
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Muscle Proteins / metabolism
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Tropomodulin
Substances
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ACTR2 protein, human
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ACTR3 protein, human
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Actin Depolymerizing Factors
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Actin-Related Protein 2
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Actin-Related Protein 3
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Actins
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CapZ Actin Capping Protein
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Carrier Proteins
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Cytoskeletal Proteins
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Gelsolin
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Microfilament Proteins
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Molecular Motor Proteins
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Muscle Proteins
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TMOD1 protein, human
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Tropomodulin