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We examined mechanisms of LPS\u2010stimulated motility and found that LPS at 100\u2009ng\/ml induced rapid elongation and ruffling of macrophage\u2010like J774 cells. A wound\u2010healing assay revealed that LPS also activated directed cell movement that was followed by TNF\u2010\u03b1 production. The CD14 and TLR4 receptors of LPS translocated to the leading lamella of polarized cells, where they transiently colocalized triggering local accumulation of actin filaments and phosphatidylinositol 4,5\u2010bisphosphate. Fractionation of Triton X\u2010100 cell lysates revealed that LPS induced polymerization of cytoskeletal actin filaments by 50%, which coincided with the peak of cell motility. This microfilament population appeared at the expense of short filaments composing the plasma membrane skeleton of unstimulated cells and actin monomers consisting prior to the LPS stimulation about 60% of cellular actin. Simultaneously with actin polymerization, LPS stimulated phosphorylation of two actin\u2010regulatory proteins, paxillin on tyrosine 118 by 80% and N\u2010WASP on serine 484\/485 by 20%, and these events preceded activation of NF\u2010\u03baB. LPS\u2010induced protein phosphorylation and reorganization of the actin cytoskeleton were inhibited by PP2, a drug affecting activity of tyrosine kinases of the Src family. The data indicate that paxillin and N\u2010WASP are involved in the reorganization of actin cytoskeleton driving motility of LPS\u2010stimulated cells. Disturbances of actin organization induced by cytochalasin D did not inhibit TNF\u2010\u03b1 production suggesting that LPS\u2010induced cell motility is not required for TNF\u2010\u03b1 release. J. Cell. Biochem. 113: 80\u201392, 2012. \u00a9 2011 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/jcb.23330","type":"journal-article","created":{"date-parts":[[2011,8,31]],"date-time":"2011-08-31T23:44:37Z","timestamp":1314834277000},"page":"80-92","source":"Crossref","is-referenced-by-count":50,"title":["LPS induces phosphorylation of actin\u2010regulatory proteins leading to actin reassembly and macrophage 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