Role for plastin in host defense distinguishes integrin signaling from cell adhesion and spreading

Immunity. 2003 Jul;19(1):95-104. doi: 10.1016/s1074-7613(03)00172-9.


Integrin ligation activates both cell adhesion and signal transduction, in part through reorganization of the actin cytoskeleton. Plastins (also known as fimbrins) are actin-crosslinking proteins of the cortical cytoskeleton present in all cells and conserved from yeast to mammals. Here we show that plastin-deficient polymorphonuclear neutrophils (PMN) are deficient in killing the bacterial pathogen Staphylococcus aureus in vivo and in vitro, despite normal phagocytosis. Like integrin beta2-deficient PMN, plastin-deficient PMN cannot generate an adhesion-dependent respiratory burst, because of markedly diminished integrin-dependent syk activation. Unlike beta2(-/-) PMN, plastin-deficient PMN adhere and spread normally. Deficiency of plastin thus separates the classical integrin receptor functions of adhesion and spreading from intracellular signal transduction.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • CD18 Antigens / physiology*
  • Cell Adhesion
  • Cell Movement
  • Enzyme Precursors / physiology
  • Immunity, Innate
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins
  • Mice
  • Mice, Inbred C57BL
  • Microfilament Proteins
  • Neutrophils / immunology*
  • Neutrophils / physiology
  • Phosphoproteins / physiology*
  • Protein-Tyrosine Kinases / physiology
  • Respiratory Burst
  • Signal Transduction / physiology*
  • Staphylococcal Infections / immunology
  • Syk Kinase


  • CD18 Antigens
  • Enzyme Precursors
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins
  • Microfilament Proteins
  • Phosphoproteins
  • plastin
  • Protein-Tyrosine Kinases
  • Syk Kinase
  • Syk protein, mouse