Herpesvirus saimiri (HVS) is an oncogenic γ-2 herpesvirus that causes lymphoma in New World primates. HVS can be further divided into subgroups A, B, and C, based on sequence divergence. Saimiri transforming protein (STP) is coded for by the first open reading frame at the left end of the HVS genome and is responsible for its oncogenic potential. Here we show that STP A11 binds to signal transducers and activators of transcription 3 (STAT3), stimulates STAT3 phosphorylation, and activates STAT3-dependent transcription. STP A11 recruited c-Src kinase to phosphorylate STAT3 protein, and co-expression of STP A11 with c-Src dramatically increased STAT3 phosphorylation. We found that the amino terminal domain of STP A11 is required for both STAT3 interaction and activation, and that physical interaction is required for STAT3 activation.
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 2004 Jul 16|
Bibliographical noteFunding Information:
This work was supported in part by grants from the National Research Laboratory Program of the Korea Institute of Science and Technology Evaluation and Planning and the BK21 Program of the Ministry of Education, Korea.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology