LMP1 structure and signal transduction.
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.
Eliopoulos
A G
AG
CRC Institute for Cancer Studies, The University of Birmingham Medical School, Birmingham, B15 2TA, UK. A.G.Eliopoulos@bham.ac.uk
Young
L S
LS
D000595:Amino Acid Sequence; D000818:Animals; D002472:Cell Transformation, Viral; D004854:Herpesvirus 4, Human / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D016328:NF-kappa B / Q000378:metabolism; D011485:Protein Binding; D015398:Signal Transduction; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000378:metabolism*
C037662:EBV-associated membrane antigen, Epstein-Barr virus; D016328:NF-kappa B; D014763:Viral Matrix Proteins; D020928:Mitogen-Activated Protein Kinases