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Heterodimer formation between c-Jun and Jun B proteins mediated by Epstein-Barr virus encoded latent membrane protein 1.
Cell Signal. 2004 Oct; 16(10):1153-62.CS

Abstract

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+Show Affiliations

Cancer Research Institute, Xiangya School of Medicine, Central South of University, 88 Xiangya Road, Changsha 410078, China.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15240010

Citation

Song, Xin, et al. "Heterodimer Formation Between c-Jun and Jun B Proteins Mediated By Epstein-Barr Virus Encoded Latent Membrane Protein 1." Cellular Signalling, vol. 16, no. 10, 2004, pp. 1153-62.
Song X, Tao YG, Deng XY, et al. Heterodimer formation between c-Jun and Jun B proteins mediated by Epstein-Barr virus encoded latent membrane protein 1. Cell Signal. 2004;16(10):1153-62.
Song, X., Tao, Y. G., Deng, X. Y., Jin, X., Tan, Y. N., Tang, M., Wu, Q., Lee, L. M., & Cao, Y. (2004). Heterodimer formation between c-Jun and Jun B proteins mediated by Epstein-Barr virus encoded latent membrane protein 1. Cellular Signalling, 16(10), 1153-62.
Song X, et al. Heterodimer Formation Between c-Jun and Jun B Proteins Mediated By Epstein-Barr Virus Encoded Latent Membrane Protein 1. Cell Signal. 2004;16(10):1153-62. PubMed PMID: 15240010.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Heterodimer formation between c-Jun and Jun B proteins mediated by Epstein-Barr virus encoded latent membrane protein 1. AU - Song,Xin, AU - Tao,Yong-Guang, AU - Deng,Xi-Yun, AU - Jin,Xin, AU - Tan,Yun-Nian, AU - Tang,Min, AU - Wu,Qiao, AU - Lee,Leo M, AU - Cao,Ya, PY - 2004/01/20/received PY - 2004/03/15/accepted PY - 2004/7/9/pubmed PY - 2005/1/20/medline PY - 2004/7/9/entrez SP - 1153 EP - 62 JF - Cellular signalling JO - Cell Signal VL - 16 IS - 10 N2 - 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. SN - 0898-6568 UR - https://www.unboundmedicine.com/medline/citation/15240010/Heterodimer_formation_between_c_Jun_and_Jun_B_proteins_mediated_by_Epstein_Barr_virus_encoded_latent_membrane_protein_1_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0898656804000476 DB - PRIME DP - Unbound Medicine ER -