Analysis of a bacterial lipopolysaccharide-activated serine kinase that phosphorylates p65/L-plastin in macrophages

Microbiology and Immunology
Akifumi HagiHiroto Shinomiya

Abstract

We previously identified p65/L-plastin as a phosphorylated protein in LPS-stimulated macrophages and determined its phosphorylation site. In vitro kinase assay using peptide substrates revealed that LPS-stimulated kinase activity selectively phosphorylated their serine-5 (Ser-5) residue. Kinase inhibitors for cAMP-dependent kinase such as H-89 inhibited the Ser-5 phosphorylation, but cAMP was not essential for the kinase activity. The LPS-stimulated kinase activity in cytosol fractions of macrophages was recovered as a sharp peak by anion exchange chromatography. These findings suggest that an as yet unknown H-89-sensitive serine kinase is rapidly activated by LPS stimulation and then phosphorylates p65/L-plastin, playing a vital role in macrophage activation.

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Citations

Jul 22, 2014·Journal of Periodontal Research·V Ö ÖztürkN Bostanci
Dec 24, 2011·International Journal of Cell Biology·Sharon Celeste Morley
Dec 4, 2015·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Maiti J LommelElisabeth Schaffner-Reckinger
Jun 20, 2007·Nihon saikingaku zasshi. Japanese journal of bacteriology·Hiroto Shinomiya

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