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pubmed-article:20140750pubmed:abstractTextRNA interference has tremendously advanced our understanding of gene function but recent reports have exposed undesirable side-effects. Recombinant Camelid single-domain antibodies (VHHs) provide an attractive means for studying protein function without affecting gene expression. We raised VHHs against gelsolin (GsnVHHs), a multifunctional actin-binding protein that controls cellular actin organization and migration. GsnVHH-induced delocalization of gelsolin to mitochondria or the nucleus in mammalian cells reveals distinct subpopulations including free gelsolin and actin-bound gelsolin complexes. GsnVHH 13 specifically recognizes Ca(2+)-activated gelsolin (K (d) approximately 10 nM) while GsnVHH 11 binds gelsolin irrespective of Ca(2+) (K (d) approximately 5 nM) but completely blocks its interaction with G-actin. Both GsnVHHs trace gelsolin in membrane ruffles of EGF-stimulated MCF-7 cells and delay cell migration without affecting F-actin severing/capping or actin nucleation activities by gelsolin. We conclude that VHHs represent a potent way of blocking structural proteins and that actin nucleation by gelsolin is more complex than previously anticipated.lld:pubmed
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pubmed-article:20140750pubmed:articleTitleA llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction.lld:pubmed
pubmed-article:20140750pubmed:affiliationDepartment of Medical Protein Research, VIB, 9000 Ghent, Belgium.lld:pubmed
pubmed-article:20140750pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:20140750pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed