Key result
Mutations in the ARPC2 and ARPC4 subunits of the Arp2/3 complex reduced actin nucleation activity up to 12-fold and decreased Y-branch half-life from 28 minutes to less than 10 minutes.
Population
Arp2/3 complex and actin filaments (computational models and purified proteins from insect cells)
Comparison
Mutagenesis of charged surface residues on ARPC2… vs Wild-type Arp2/3 complex
Design
Preclinical
Authors
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Highlights ARPC2/ARPC4 roles in actin dynamics; leaves open cardiovascular cytoskeletal implications.
Computational and biochemical analyses identify a specific surface on the Arp2/3 complex critical for F-actin binding, nucleation, and branch stability.
Goley et al. (2010) studied this question. Mutagenesis of ARPC2 and ARPC4 subunits vs. Wild-type Arp2/3 complex was evaluated on Actin nucleation activity and Y-branch stability. Mutations in the ARPC2 and ARPC4 subunits of the Arp2/3 complex reduced actin nucleation activity up to 12-fold and decreased Y-branch half-life from 28 minutes to less than 10 minutes.
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