Source:http://linkedlifedata.com/resource/pubmed/id/17947705
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2007-10-19
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pubmed:abstractText |
Monarch-1/NLRP12 is expressed in myeloid cells and functions as a negative regulator of inflammation by inducing proteasome-mediated degradation of NF-kappaB-inducing kinase. Monarch-1 is a member of the CATERPILLER gene family, also known as the nucleotide-binding domain leucine-rich repeat gene family. This family shares strong structural homology to major immune regulators expressed in lower organisms, including plants. In plants, these disease-resistance proteins (R proteins) sense pathogenic insult and initiate a protective response to limit pathogen growth. To perform this role, many R proteins require the highly conserved chaperone molecule, heat shock protein (Hsp) 90. Using a two-dimensional gel/mass spectrometry system, we detected the association of the nucleotide-binding domain leucine-rich repeat protein Monarch-1 with heat shock proteins. Further analysis indicates that analogous to plant R proteins, Hsp90 is required for Monarch-1 activity. In human monocytes, Monarch-1 associates with Hsp90, and these complexes are sensitive to treatment with specific Hsp90 inhibitors. Disruption of these complexes results in rapid degradation of Monarch-1 via the proteasome and prevents Monarch-1-induced proteolysis of NF-kappaB-inducing kinase. This demonstrates that Hsp90 is a critical regulator of Monarch-1 anti-inflammatory activity.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/AI063031,
http://linkedlifedata.com/resource/pubmed/grant/DE016326,
http://linkedlifedata.com/resource/pubmed/grant/DK38108,
http://linkedlifedata.com/resource/pubmed/grant/SERCEB A1-02-031,
http://linkedlifedata.com/resource/pubmed/grant/T32-A1007273-22
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B kinase,
http://linkedlifedata.com/resource/pubmed/chemical/NLRP12 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
179
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6291-6
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:17947705-Cells, Cultured,
pubmed-meshheading:17947705-HSP70 Heat-Shock Proteins,
pubmed-meshheading:17947705-HSP90 Heat-Shock Proteins,
pubmed-meshheading:17947705-Humans,
pubmed-meshheading:17947705-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:17947705-Monocytes,
pubmed-meshheading:17947705-Proteasome Endopeptidase Complex,
pubmed-meshheading:17947705-Protein Binding,
pubmed-meshheading:17947705-Protein-Serine-Threonine Kinases,
pubmed-meshheading:17947705-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2007
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pubmed:articleTitle |
Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase.
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pubmed:affiliation |
Department of Microbiology and Immunology, Cancer Center, University of North Carolina, Chapel Hill, NC 27599, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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