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  Molecular basis of phosphorylation-induced activation of the NADPH oxidase

Groemping, Y., Lapouge, K., Smerdon, S. J., & Rittinger, K. (2003). Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell, 113(3), 343-355. doi:10.1016/S0092-8674(03)00314-3.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0000-3CAE-A Version Permalink: https://hdl.handle.net/21.11116/0000-0000-3CAF-9
Genre: Journal Article

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Cell_113_2003_343.pdf (Any fulltext), 681KB
 
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Groemping, Yvonne1, Author           
Lapouge, Karin, Author
Smerdon, Stephen J., Author
Rittinger, Katrin2, Author           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: The multi-subunit NADPH oxidase complex plays a crucial role in host defense against microbial infection through the production of reactive oxygen species. Activation of the NADPH oxidase requires the targeting of a cytoplasmic p40-p47-p67(phox) complex to the membrane bound heterodimeric p22-gp91(phox) flavocytochrome. This interaction is prevented in the resting state due to an auto-inhibited conformation of p47(phox). The X-ray structure of the auto-inhibited form of p47(phox) reveals that tandem SH3 domains function together to maintain the cytoplasmic complex in an inactive form. Further structural and biochemical data show that phosphorylation of p47(phox) activates a molecular switch that relieves the inhibitory intramolecular interaction. This permits p47(phox) to interact with the cytoplasmic tail of p22(phox) and initiate formation of the active, membrane bound enzyme complex.

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Language(s): eng - English
 Dates: 2003-03-052002-10-232003-03-312003-04-152003-05-02
 Publication Status: Issued
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0092-8674(03)00314-3
URI: http://www.ncbi.nlm.nih.gov/pubmed/12732142
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Title: Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 113 (3) Sequence Number: - Start / End Page: 343 - 355 Identifier: ISSN: 0092-8674
CoNE: https://pure.mpg.de/cone/journals/resource/954925463183