Linked Life Data

11796733

Source:http://linkedlifedata.com/resource/pubmed/id/11796733

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2002-3-18
pubmed:abstractText
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).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10121-8
pubmed:dateRevised
2006-4-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Architecture of the p40-p47-p67phox complex in the resting state of the NADPH oxidase. A central role for p67phox.
pubmed:affiliation
Division of Protein Structure, National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom.
pubmed:publicationType
Journal Article