Document Detail


Heterodimer formation between c-Jun and Jun B proteins mediated by Epstein-Barr virus encoded latent membrane protein 1.
MedLine Citation:
PMID:  15240010     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Epstein-Barr virus (EBV) encoded latent membrane protein 1 (LMP1) is essential for the immortalization of human B cells and is linked etiologically to several human tumors. LMP1 is an integral membrane protein which acts like a constitutively active receptor. It binds tumor necrosis factor (TNF)-receptor-associated factors (TRAFs), activates NFkappaB and triggers the transcription factor activating protein-1 (AP-1) via the c-Jun N-terminal kinase (JNK) cascade, but its specific contribution to AP-1 has not been elucidated fully. Members of AP-1 family, the Jun and fos related protein, have been shown to directly interact and form heterodimeric complexes. In this report, using a Tet-on LMP1 HNE2 cell line which is a dual-stable LMP1 integrated nasopharyngeal carcinoma (NPC) cell line and the expression of LMP1 in which could be regulated by Tet-on system, we show that Jun B can efficiently form a new heterodimeric complex with the c-Jun protein under the regulation of LMP1, phosphorylation of c-Jun (ser63, ser73) and Jun B involved in the process of the new heterodimeric form. We also find that this heterodimeric form can bind to the AP-1 consensus sequence. Transfection studies suggest that JNK interaction protein (JIP) could inhibit the heterodimer form of c-Jun and Jun B through blocking the AP-1 signaling pathway triggered by LMP1. The interaction and function between c-Jun protein and Jun B protein increase the repertoire of possible regulatory complexes by LMP1 that could play an important role in the regulation of transcription of specific cellular genes in the process of genesis of nasopharyngeal carcinoma.
Authors:
Xin Song; Yong-Guang Tao; Xi-Yun Deng; Xin Jin; Yun-Nian Tan; Min Tang; Qiao Wu; Leo M Lee; Ya Cao
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cellular signalling     Volume:  16     ISSN:  0898-6568     ISO Abbreviation:  Cell. Signal.     Publication Date:  2004 Oct 
Date Detail:
Created Date:  2004-07-08     Completed Date:  2005-01-19     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8904683     Medline TA:  Cell Signal     Country:  England    
Other Details:
Languages:  eng     Pagination:  1153-62     Citation Subset:  IM    
Affiliation:
Cancer Research Institute, Xiangya School of Medicine, Central South of University, 88 Xiangya Road, Changsha 410078, China.
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MeSH Terms
Descriptor/Qualifier:
Dimerization
Humans
JNK Mitogen-Activated Protein Kinases / metabolism*
Nasopharyngeal Neoplasms / metabolism
Phosphorylation
Proto-Oncogene Proteins c-jun / metabolism*
Signal Transduction / physiology*
Transcription Factor AP-1 / metabolism*
Tumor Cells, Cultured
Viral Matrix Proteins / metabolism*
Chemical
Reg. No./Substance:
0/EBV-associated membrane antigen, Epstein-Barr virus; 0/Proto-Oncogene Proteins c-jun; 0/Transcription Factor AP-1; 0/Viral Matrix Proteins; EC 2.7.11.24/JNK Mitogen-Activated Protein Kinases

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