Priming-induced localization of G(ialpha2) in high density membrane microdomains.
Biochem Biophys Res Commun
; 301(4): 862-72, 2003 Feb 21.
Article
en En
| MEDLINE
| ID: mdl-12589792
ABSTRACT
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.
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Colección:
01-internacional
Asunto principal:
Membrana Celular
/
Proteínas Proto-Oncogénicas
/
Subunidades alfa de la Proteína de Unión al GTP Gi-Go
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2003
Tipo del documento:
Article
País de afiliación:
Estados Unidos