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PMID: 11669605 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

LMP1 structure and signal transduction.

Seminars in cancer biology ·Vol. 11 ·No. 6 ·2001-12-00 ·Pages 435-44

Eliopoulos AG, Young LS

Abstract

The oncogenic Epstein-Barr virus (EBV)-encoded latent membrane protein 1 (LMP1) has structural features and functions reminiscent of a constitutively active TNF family receptor. LMP1 aggregates at the plasma membrane and initiates the activation of signalling pathways, such as NF- kappa B, the mitogen-activated protein kinases JNK and p38, the small GTPase Cdc42 and the JAK/STAT cascade. The constitutive engagement of these signals and the characteristic molecular interactions that regulate them provide the basis for the molecular explanation of the transforming properties of this key EBV protein.

MeSH Terms
Amino Acid Sequence Animals Cell Transformation, Viral Herpesvirus 4, Human/chemistry,metabolism Humans Mitogen-Activated Protein Kinases/metabolism NF-kappa B/metabolism Protein Binding Signal Transduction Viral Matrix Proteins/chemistry,metabolism
Chemicals
EBV-associated membrane antigen, Epstein-Barr virus NF-kappa B Viral Matrix Proteins Mitogen-Activated Protein Kinases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Eliopoulos A G
CRC Institute for Cancer Studies, The University of Birmingham Medical School, Birmingham, B15 2TA, UK. [email protected]
Young L S
Article Info
Journal
Seminars in cancer biology
Abbr.
Semin Cancer Biol
ISSN
1044-579X
Published
2001-12-00
Pages
435-44
Language
English
Region
England
NLM ID
9010218
Subset
IM
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