Open AccessArp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function
Author(s) -
Alessia Di Nardo,
Gregor Cicchetti,
Hervé Falet,
John H. Hartwig,
Thomas P. Stossel,
David J. Kwiatkowski
Publication year - 2005
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0508228102
Subject(s) - microbiology and biotechnology , lamellipodium , membrane ruffling , wiskott–aldrich syndrome protein , biology , actin , actin remodeling , cofilin , pseudopodia , motility , actin cytoskeleton , cytoskeleton , cell , biochemistry
RNA interference silencing of up to 90% of Arp3 protein expression, a major subunit of the Arp2/3 complex, proportionately decreases the intracellular motility ofListeria monocytogenes and actin nucleation activity ascribable to the Arp2/3 complex in mouse embryonic fibroblasts. However, the Arp2/3-deficient cells exhibit unimpaired lamellipodial actin network structure, translational locomotion, spreading, actin assembly, and ruffling responses. In addition, Arp3-silenced cells expressing neural Wiskott-Aldrich syndrome protein-derived peptides that inhibit Arp2/3 complex function in wild-type cells retained normal PDGF-induced ruffling. The Arp2/3 complex can be dispensable for leading-edge actin remodeling.
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