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Assembly of the Phagocyte NADPH Oxidase: Binding of Src Homology 3 Domains to Proline-Rich Targets

Leto, Thomas L. ; Adams, Anthony G. ; de Mendez, Isabelle

Proceedings of the National Academy of Sciences - PNAS, 1994-10, Vol.91 (22), p.10650-10654 [Periódico revisado por pares]

United States: National Academy of Sciences of the United States of America

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Título:
Assembly of the Phagocyte NADPH Oxidase: Binding of Src Homology 3 Domains to Proline-Rich Targets
Autor: Leto, Thomas L. ; Adams, Anthony G. ; de Mendez, Isabelle
Assuntos: Amino Acid Sequence ; Animals ; B lymphocytes ; B-Lymphocytes - metabolism ; Binding Sites ; Biochemistry ; Cell Line ; Cell lines ; Complementary DNA ; Consensus Sequence ; Cytochrome b Group - metabolism ; Cytochromes ; DNA Primers ; Enzyme Activation ; Enzymes ; Genes, src ; Granulomatous Disease, Chronic - genetics ; Granulomatous Disease, Chronic - metabolism ; Humans ; K562 cells ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; NADH, NADPH Oxidoreductases - biosynthesis ; NADPH Dehydrogenase - metabolism ; NADPH Oxidases ; Neutrophils ; Oxidases ; Phagocytes - enzymology ; Phosphoproteins - metabolism ; Point Mutation ; Polymerase Chain Reaction ; Proline ; Protein Binding ; Proteins ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - metabolism ; Sequence Homology, Amino Acid ; Spodoptera ; Superoxides ; Transfection
É parte de: Proceedings of the National Academy of Sciences - PNAS, 1994-10, Vol.91 (22), p.10650-10654
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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Descrição: The NADPH oxidase responsible for generation of superoxide anion and related microbicidal oxidants by phagocytes is assembled from at least five distinct proteins. Two are cytosolic components (p47-phox and p67-phox) that contain Src homology 3 (SH3) domains and associate with a transmembrane cytochrome b558upon activation. We show here that the SH3 domains of p47-phox bind to proline-rich sequences in p47-phox itself and the p22-phox subunit of cytochrome b558. Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156→ Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox. Expression of mutated p22-phox did not restore oxidase activity to p22-phox-deficient B cells and did not enable p22-phox-dependent translocation of p47-phox to membranes in phorbol ester-stimulated cells. We also show that the cytosolic oxidase components associate with one another through the C-terminal SH3 domain of p67-phox and a proline-rich C-terminal sequence in p47-phox. These SH3 target sites conform to consensus features deduced from SH3 binding sites in other systems. We propose a model in which the oxidase complex assembles through a mechanism involving SH3 domains of both cytosolic proteins and cognate proline-rich targets in other oxidase components.
Editor: United States: National Academy of Sciences of the United States of America
Idioma: Inglês

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Assembly of the Phagocyte NADPH Oxidase: Binding of Src Homology 3 Domains to Proline-Rich Targets

Leto, Thomas L. ; Adams, Anthony G. ; de Mendez, Isabelle

United States: National Academy of Sciences of the United States of America

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