Phosphorylation of p67 phox in the neutrophil occurs in the cytosol and is independent of p47 phox

Louisa V. Forbes; Stephen J. Moss; Anthony W. Segal

doi:10.1016/S0014-5793(99)00444-5

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Phosphorylation of p67 phox in the neutrophil occurs in the cytosol and is independent of p47 phox

Journal article

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Phosphorylation of p67 phox in the neutrophil occurs in the cytosol and is independent of p47 phox

Louisa V. Forbes, Stephen J. Moss and Anthony W. Segal

FEBS letters, Vol.449(2), pp.225-229

23/04/1999

DOI: https://doi.org/10.1016/S0014-5793(99)00444-5

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https://hdl.handle.net/10523/35598

Abstract

Nicotinamide adenine dinucleotide phosphate, reduced form oxidase

Phosphopeptide mapping

Phosphorylation

p67 phox and p47 phox are phosphorylated in the course of stimulation of the NADPH oxidase in neutrophils. Isolated neutrophil cytosol can phosphorylate both of these proteins in vitro. Phosphoamino acid analysis showed that isolated membranes can tyrosine-phosphorylate p67 phox in vitro. Further experiments with anti-phosphotyrosine antibodies did not support a role for tyrosine phosphorylation of p67 phox in the cell. A phosphopeptide analysis showed that the phosphorylation of p67 phox is unchanged in the absence of p47 phox. These results further characterise the phosphorylation of p67 phox and provide evidence that this is a cytosolic event independent of interaction with p47 phox and the membrane.

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Record Identifier: 9926518228701891
Title: Phosphorylation of p67 phox in the neutrophil occurs in the cytosol and is independent of p47 phox
Creators: Louisa V. Forbes
Stephen J. Moss
Anthony W. Segal
Publication Details: FEBS letters, Vol.449(2), pp.225-229
Academic Unit: Pathology and Molecular Medicine (UOC)
Publisher: Elsevier B.V
Date published ; e-published: 23/04/1999
Language: English
Resource Type ; Subtype: Journal article