Regulation of human leukocyte p21-activated kinases through G protein-coupled receptors

Ulla G. Knaus, Sharron Morris, Hui Jia Dong, Jonathan Chernoff, Gary M. Bokoch

Research output: Contribution to journalArticlepeer-review

366 Scopus citations

Abstract

The Rac guanosine 5′-triphosphate (GTP)-binding proteins regulate oxidant production by phagocytic leukocytes. Two Ste20-related p21-activated kinases (PAKs) were identified as targets of Rac in human neutrophils. Activity of the ∼65- and ∼68-kilodalton PAKs was rapidly stimulated by chemoattractants acting through pertussis toxin-sensitive heterotrimeric GTP-binding proteins (G proteins). Native and recombinant PAKs phosphorylated the p47phox reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase component in a Rac-GTP-dependent manner. The action of PAKs during phagocyte activation by G protein-coupled pathways may contribute to regulation of NADPH oxidase activity.

Original languageEnglish
Pages (from-to)221-223
Number of pages3
JournalScience
Volume269
Issue number5221
DOIs
StatePublished - 1995

Keywords

  • Adenosine Triphosphate/metabolism
  • Enzyme Activation
  • GTP-Binding Proteins/metabolism
  • Guanosine Triphosphate/metabolism
  • Humans
  • N-Formylmethionine Leucyl-Phenylalanine/pharmacology
  • NADH, NADPH Oxidoreductases/metabolism
  • NADPH Dehydrogenase/metabolism
  • NADPH Oxidases
  • Neutrophil Activation
  • Neutrophils/enzymology
  • Pertussis Toxin
  • Phosphoproteins/metabolism
  • Phosphorylation
  • Protein Serine-Threonine Kinases/metabolism
  • Recombinant Proteins/metabolism
  • Tetradecanoylphorbol Acetate/pharmacology
  • Virulence Factors, Bordetella/pharmacology
  • p21-Activated Kinases
  • rac GTP-Binding Proteins

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