PubMed:10357818 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/10357818","sourcedb":"PubMed","sourceid":"10357818","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/10357818","text":"Latent membrane protein 1 of Epstein-Barr virus interacts with JAK3 and activates STAT proteins.\nLatent membrane protein 1 (LMP1) acts like a permanently activated receptor of the tumor necrosis factor (TNF)-receptor superfamily and is absolutely required for B cell immortalization by Epstein-Barr virus. Molecular and biochemical approaches demonstrated that LMP1 usurps cellular signaling pathways resulting in the induction of NF-kappaB and AP-1 via two C-terminal activating regions. We demonstrate here that a third region encompassing a proline rich sequence within the 33 bp repetitive stretch of LMP1's C-terminus is required for the activation of Janus kinase 3 (JAK3). The interaction of LMP1 and JAK3 leads to the enhanced tyrosine auto/transphosphorylation of JAK3 within minutes after crosslinking of a conditional NGF-R:LMP1 chimera and is a prerequisite for the activation of STAT transcription factors. These results reveal a novel activating region in the LMP1 C-terminus and identify the JAK/STAT pathway as a target of this viral integral membrane protein in B 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