A role for the actin-bundling proteinl-plastin in the regulation of leukocyte integrin function

• DOI: 10.1073/pnas.95.16.9331
• Publication Date: 2002-07-26T14:35:50Z
• Authors: Samuel L. Jones; Jun Wang; Christoph W. Turck; Eric J. Brown
• Keywords: Integrins; 0303 health sciences; Membrane Glycoproteins; Neutrophils; Microfilament Proteins; Molecular Sequence Data; Phosphoproteins; 3. Good health; Phosphatidylinositol 3-Kinases; 03 medical and health sciences; Cell Adhesion; Serine; Humans; Amino Acid Sequence; Phosphorylation; Protein Kinase C; Signal Transduction

Regulation of leukocyte integrin avidity is a crucial aspect inflammation and immunity. The actin cytoskeleton has an important role in the regulation function, but cytoskeletal proteins involved are largely unknown. Because inflammatory stimuli that activate integrin-mediated adhesion human polymorphonuclear neutrophils (PMN) monocytes cause phosphorylation actin-bundling protein l -plastin, we tested whether -plastin was activation. -plastin-derived peptides included site (Ser-5) rapidly induced when introduced into cytosol freshly isolated primary PMN monocytes. Substitution Ala for Ser-5 abolished ability peptide to induce adhesion. Peptide-induced sensitive pharmacologic inhibition phosphoinositol 3-kinase kinase C, by containing phosphoserine at position 5 insensitive inhibition. These data establish novel suggest many signaling events implicated act via induction phosphorylation.