Priming-induced localization of Giα2 in high density membrane microdomains

Michael L. Keil, Naveenraj L. Solomon, Irfan J. Lodhi, Kimberley C. Stone, Algirdas J. Jesaitis, Peter S. Chang, Jennifer J. Linderman, Geneva M. Omann

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Subcellular fractionation of human neutrophils on linear sucrose density gradients was utilized to test the hypothesis that priming regulates the subcellular and sub-plasma membrane distribution of neutrophil G-protein subunits, Giα2 and Giα3, N-formyl peptide receptor, Lyn kinase and phospholipase Cβ2. Giα2, but not Giα3, moved from a lighter to a higher density plasma membrane fraction. Unoccupied N-formyl peptide receptors were found throughout the plasma membrane fractions and this distribution did not change with priming. In unprimed cells Giα2 and its effector, phospholipase Cβ2, were segregated in different membrane compartments; priming caused Giα2 to move to the compartment in which phospholipase Cβ2 resided. Thus, an important component of the mechanism of priming may involve regulation of the location of G-proteins and effector molecules in plasma membrane compartments where their abilities to couple may be enhanced.

Original languageEnglish
Pages (from-to)862-872
Number of pages11
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Feb 21 2003


  • Cellular activation
  • Lipid rafts
  • Lipopolysaccharide
  • Membrane microdomains
  • Neutrophils
  • Recombinant human tumor necrosis factor α
  • Signal transduction


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