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  Architecture of the p40-p47-p67phox complex in the resting state of the NADPH oxidase. A central role for p67phox.

Lapouge, K., Smith, S. J. M., Groemping, Y., & Rittinger, K. (2002). Architecture of the p40-p47-p67phox complex in the resting state of the NADPH oxidase. A central role for p67phox. The Journal of Biological Chemistry, 277(12), 10121-10128. doi:10.1074/jbc.M112065200.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-141E-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-141F-6
Genre: Journal Article

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JBiolChem_277_2002_10121.pdf (Any fulltext), 255KB
 
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 Creators:
Lapouge, Karin, Author
Smith, Susan J. M., Author
Groemping, Yvonne1, 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 phagocyte NADPH oxidase is a multiprotein enzyme whose subunits are partitioned between the cytosol and plasma membrane in resting cells. Upon exposure to appropriate stimuli multiple phosphorylation events in the cytosolic components take place, which induce rearrangements in a number of protein-protein interactions, ultimately leading to translocation of the cytoplasmic complex to the membrane. To understand the molecular mechanisms that underlie the assembly and activation process we have carried out a detailed study of the protein-protein interactions that occur in the p40-p47-p67(phox) complex of the resting oxidase. Here we show that this complex contains one copy of each protein, which assembles to form a heterotrimeric complex. The apparent high molecular weight of this complex, as observed by gel filtration studies, is due to an extended, non-globular shape rather than to the presence of multiple copies of any of the proteins. Isothermal titration calorimetry measurements of the interactions between the individual components of this complex demonstrate that p67(phox) is the primary binding partner of p47(phox) in the resting state. These findings, in combination with earlier reports, allow us to propose a model for the architecture of the resting complex in which p67(phox) acts as the bridging molecule that connects p40(phox) and p47(phox).

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Language(s): eng - English
 Dates: 2001-12-182002-01-152002-01-162002-03-22
 Publication Status: Published in print
 Pages: 8
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 Rev. Method: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 277 (12) Sequence Number: - Start / End Page: 10121 - 10128 Identifier: ISSN: 0021-9258
CoNE: /journals/resource/954925410826_1