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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0031715,
umls-concept:C0185117,
umls-concept:C0205263,
umls-concept:C0248813,
umls-concept:C0670896,
umls-concept:C0699040,
umls-concept:C1419881,
umls-concept:C1825546,
umls-concept:C1879547,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
2010-7-8
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pubmed:abstractText |
The presentation of the endoplasmic reticulum resident chaperone protein, gp96 on the cell surface have been considered as a phenomenon of the immunogenic process activation. Previously, we showed aminoacyl-tRNA synthetase-interacting multifunctional protein 1 (AIMP1) can form a molecular complex with gp96, regulate the ER retention of gp96 through KDEL receptor, and suppress its cell surface expression. However, the physiological conditions that modulate AIMP1-gp96 interaction and cell surface expression of gp96 are not known. In this study, we investigated the process that which can modulate dissociation of AIMP1 and gp96 by using Toll-like receptor (TLR) activation. MyD88 pathway by LPS-mediated TLR4 activation induced the cell surface presentation of gp96 through c-Jun N-terminal kinase (JNK). AIMP1 was phosphorylated by JNK upon LPS stimulation and gp96 was dissociated from phosphorylated AIMP1. We further demonstrated that serine-140 residue of AIMP1 was phosphorylated by JNK and alanine mutation of serine-140 suppressed LPS-induced cell surface expression of gp96. Altogether, these results suggest that AIMP1 is phosphorylated by JNK through TLR-MyD88 pathway and lose the regulatory activity for ER retention of gp96, resulting in the increase of cell surface expression of gp96, and provide a new molecular mechanism underlying TLR-mediated gp96 regulation.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/MYD88 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Myeloid Differentiation Factor 88,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/TLR4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 4,
http://linkedlifedata.com/resource/pubmed/chemical/sarcoma glycoprotein gp96...,
http://linkedlifedata.com/resource/pubmed/chemical/small inducible cytokine subfamily...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1090-2104
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pubmed:author |
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pubmed:copyrightInfo |
Copyright (c) 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
397
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
100-5
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pubmed:meshHeading |
pubmed-meshheading:20510162-Antigens, Neoplasm,
pubmed-meshheading:20510162-Cell Membrane,
pubmed-meshheading:20510162-Cytokines,
pubmed-meshheading:20510162-Endoplasmic Reticulum,
pubmed-meshheading:20510162-Enzyme Activation,
pubmed-meshheading:20510162-HL-60 Cells,
pubmed-meshheading:20510162-Humans,
pubmed-meshheading:20510162-Immunity, Innate,
pubmed-meshheading:20510162-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:20510162-Lipopolysaccharides,
pubmed-meshheading:20510162-Molecular Chaperones,
pubmed-meshheading:20510162-Mutation,
pubmed-meshheading:20510162-Myeloid Differentiation Factor 88,
pubmed-meshheading:20510162-Neoplasm Proteins,
pubmed-meshheading:20510162-Phosphorylation,
pubmed-meshheading:20510162-RNA-Binding Proteins,
pubmed-meshheading:20510162-Serine,
pubmed-meshheading:20510162-Toll-Like Receptor 4
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pubmed:year |
2010
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pubmed:articleTitle |
Toll-like receptor 4-mediated c-Jun N-terminal kinase activation induces gp96 cell surface expression via AIMP1 phosphorylation.
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pubmed:affiliation |
Center for Medicinal Protein Network and Systems Biology, College of Pharmacy, Seoul National University, Seoul, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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