Herpesvirus saimiri STP A11 protein interacts with STAT3 and stimulates its transcriptional activity

Junsoo Park, Taegun Seo, Jun Jung, Joonho Choe

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)279-285
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume320
Issue number1
DOIs
Publication statusPublished - 2004 Jul 16

Fingerprint

Saimiriine Herpesvirus 2
STAT3 Transcription Factor
Saimiri
Proteins
Phosphorylation
Chemical activation
STAT Transcription Factors
Herpesviridae
Transcription
Primates
Transcriptional Activation
Open Reading Frames
Lymphoma
Genes
Genome

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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Herpesvirus saimiri STP A11 protein interacts with STAT3 and stimulates its transcriptional activity. / Park, Junsoo; Seo, Taegun; Jung, Jun; Choe, Joonho.

In: Biochemical and Biophysical Research Communications, Vol. 320, No. 1, 16.07.2004, p. 279-285.

Research output: Contribution to journalArticle

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