Priming-induced localization of G(ialpha2) in high density membrane microdomains

• Published in: Biochemical and biophysical research communications Vol. 301; no. 4; pp. 862 - 872
• Main Authors: Keil, Michael L, Solomon, Naveenraj L, Lodhi, Irfan J, Stone, Kimberley C, Jesaitis, Algirdas J, Chang, Peter S, Linderman, Jennifer J, Omann, Geneva M
• Format: Journal Article
• Language: English
• Published: United States 21.02.2003
• Subjects: Alkaline Phosphatase - metabolism; Cell Compartmentation; Cell Membrane - metabolism; Cytosol - metabolism; GTP-Binding Protein alpha Subunit, Gi2; GTP-Binding Protein alpha Subunits, Gi-Go - metabolism; Heterotrimeric GTP-Binding Proteins - metabolism; Isoenzymes - metabolism; Lipopolysaccharides - pharmacology; Membrane Microdomains - metabolism; Models, Biological; NADPH Oxidases - metabolism; Neutrophils - drug effects; Neutrophils - metabolism; Phospholipase C beta; Proto-Oncogene Proteins - metabolism; Receptors, Formyl Peptide; Receptors, Immunologic - metabolism; Receptors, Peptide - metabolism; Signal Transduction; src-Family Kinases - metabolism; Tumor Necrosis Factor-alpha - pharmacology; Type C Phospholipases - metabolism
• ISSN: 0006-291X
• DOI: 10.1016/S0006-291X(03)00057-3

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, G(ialpha2) and G(ialpha3), N-formyl peptide receptor, Lyn kinase and phospholipase C(beta2). G(ialpha2), but not G(ialpha3), 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 G(ialpha2) and its effector, phospholipase C(beta2), were segregated in different membrane compartments; priming caused G(ialpha2) to move to the compartment in which phospholipase C(beta2) 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.