pubmed-article:20510162 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C0248813 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C0670896 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C1419881 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C1825546 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:20510162 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:20510162 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:20510162 | pubmed:dateCreated | 2010-7-8 | lld:pubmed |
pubmed-article:20510162 | 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. | lld:pubmed |
pubmed-article:20510162 | pubmed:language | eng | lld:pubmed |
pubmed-article:20510162 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20510162 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20510162 | pubmed:month | Jun | lld:pubmed |
pubmed-article:20510162 | pubmed:issn | 1090-2104 | lld:pubmed |
pubmed-article:20510162 | pubmed:author | pubmed-author:KimSunghoonS | lld:pubmed |
pubmed-article:20510162 | pubmed:author | pubmed-author:HanJung MinJM | lld:pubmed |
pubmed-article:20510162 | pubmed:author | pubmed-author:KimGyuyoupG | lld:pubmed |
pubmed-article:20510162 | pubmed:copyrightInfo | Copyright (c) 2010 Elsevier Inc. All rights reserved. | lld:pubmed |
pubmed-article:20510162 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20510162 | pubmed:day | 18 | lld:pubmed |
pubmed-article:20510162 | pubmed:volume | 397 | lld:pubmed |
pubmed-article:20510162 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20510162 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20510162 | pubmed:pagination | 100-5 | lld:pubmed |
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pubmed-article:20510162 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20510162 | pubmed:articleTitle | Toll-like receptor 4-mediated c-Jun N-terminal kinase activation induces gp96 cell surface expression via AIMP1 phosphorylation. | lld:pubmed |
pubmed-article:20510162 | pubmed:affiliation | Center for Medicinal Protein Network and Systems Biology, College of Pharmacy, Seoul National University, Seoul, Republic of Korea. | lld:pubmed |
pubmed-article:20510162 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20510162 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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