Arp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function.
RNA interference silencing of up to 90% of Arp3 protein expression, a major subunit of the Arp2/3 complex, proportionately decreases the intracellular motility of Listeria 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.
Di Nardo
Alessia
A
Division of Hematology, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, One Blackfan Circle, Boston, MA 02115, USA.
Cicchetti
Gregor
G
Falet
Hervé
H
Hartwig
John H
JH
Stossel
Thomas P
TP
Kwiatkowski
David J
DJ
D051376:Actin-Related Protein 2-3 Complex / Q000235:genetics / Q000502:physiology*; D000199:Actins / Q000737:chemistry* / Q000502:physiology; D000818:Animals; D002478:Cells, Cultured; D005347:Fibroblasts / Q000502:physiology; D020868:Gene Silencing; D051379:Mice; D010982:Platelet-Derived Growth Factor / Q000494:pharmacology; D034622:RNA Interference
D051376:Actin-Related Protein 2-3 Complex; D000199:Actins; D010982:Platelet-Derived Growth Factor