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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2008-1-18
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pubmed:abstractText |
NEMO is an essential regulatory component of the IkappaB kinase (IKK) complex, which controls activation of the NF-kappaB signaling pathway. Herein, we show that NEMO exists as a disulfide-bonded dimer when isolated from several cell types and analyzed by SDS-polyacrylamide gel electrophoresis under non-reducing conditions. Treatment of cells with hydrogen peroxide (H(2)O(2)) induces further formation of NEMO dimers. Disulfide bond-mediated formation of NEMO dimers requires Cys54 and Cys347. The ability of these residues to form disulfide bonds is consistent with their location in a NEMO dimer structure that we generated by molecular modeling. We also show that pretreatment with H(2)O(2) decreases TNFalpha-induced IKK activity in NEMO-reconstituted cells, and that TNFalpha has a diminished ability to activate NF-kappaB DNA binding in cells reconstituted with NEMO mutant C54/347A. This study implicates NEMO as a target of redox regulation and presents the first structural model for the NEMO protein.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-11470788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-11479295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-11877453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-11971183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-11983854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-12192055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-12227765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-12483529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-12612076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-12815168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-15107419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-16246123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-16360644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-16379012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-16987664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-17000764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-17072324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-17072325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-17419723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18164680-17924664
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1090-2104
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
29
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pubmed:volume |
367
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
103-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:18164680-Animals,
pubmed-meshheading:18164680-Base Sequence,
pubmed-meshheading:18164680-Cell Nucleus,
pubmed-meshheading:18164680-Cells, Cultured,
pubmed-meshheading:18164680-Cysteine,
pubmed-meshheading:18164680-DNA,
pubmed-meshheading:18164680-Dimerization,
pubmed-meshheading:18164680-Disulfides,
pubmed-meshheading:18164680-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:18164680-Hydrogen Peroxide,
pubmed-meshheading:18164680-I-kappa B Kinase,
pubmed-meshheading:18164680-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:18164680-Mice,
pubmed-meshheading:18164680-Models, Molecular,
pubmed-meshheading:18164680-Mutation,
pubmed-meshheading:18164680-Oxidation-Reduction,
pubmed-meshheading:18164680-Protein Binding,
pubmed-meshheading:18164680-Tumor Necrosis Factor-alpha
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pubmed:year |
2008
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pubmed:articleTitle |
Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347.
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pubmed:affiliation |
Department of Biology, Boston University, 5 Cummington Street, Boston, MA 02215, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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