An SH3 domain and proline-rich sequence mediate an interaction between 2 components of the phagocyte NADPH oxidase complex

Finan, Peter, Shimizu, Yazuaki, Gout, Ivan, Hsuan, Justin, Truong, Oanh, Butcher, Christopher, Bennett, Paul, Waterfield, Michael D. and Kellie, Stuart (1994) An SH3 domain and proline-rich sequence mediate an interaction between 2 components of the phagocyte NADPH oxidase complex. Journal of Biological Chemistry, 269 19: 13752-13755.

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Author Finan, Peter
Shimizu, Yazuaki
Gout, Ivan
Hsuan, Justin
Truong, Oanh
Butcher, Christopher
Bennett, Paul
Waterfield, Michael D.
Kellie, Stuart
Title An SH3 domain and proline-rich sequence mediate an interaction between 2 components of the phagocyte NADPH oxidase complex
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 1994-05-13
Sub-type Letter to editor, brief commentary or brief communication
Open Access Status File (Publisher version)
Volume 269
Issue 19
Start page 13752
End page 13755
Total pages 4
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
Neutrophils possess a multicomponent NADPH oxidase system capable of producing large quantities of superoxide in a process known as the respiratory burst (1). Upon stimulation of a phagocytic cell, two cytosolic components of the oxidase, p67phox and p47phox, associate with a membrane-bound flavocytochrome b and a small GTP-binding protein to form a functional enzyme complex. Each of the Phox proteins contains two src homology 3 (SH3) domains, which are of unknown function but are potential mediators of protein-protein interactions between components of the activated oxidase. We have isolated a 47-kDa protein from lysates of differentiated HL60 cells that specifically bound to the carboxyl-terminal SH3 domain of p67phox and not to any other SH3 domain tested. This protein was identified as p47phox, and the putative SH3 domain binding site was located to a carboxyl-terminal proline-rich region. Proline-rich synthetic peptides based on this carboxyl-terminal region specifically inhibited the binding of p47phox to the carboxyl-terminal SH3 domain of p67phox, and sequential truncation defined a unique minimal sequence, which, although similar, does not match the consensus sequence defined for other SH3-binding proteins.
Q-Index Code CX
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Letter to editor, brief commentary or brief communication
Collection: School of Chemistry and Molecular Biosciences
 
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