Phorbol esters modulate the phosphorylation of human T-cell leukemia virus type I Tax

Joseph D. Fontes, Judith M. Strawhecker, Nathan D. Bills, Robert E Lewis, Steven Heye Hinrichs

Research output: Contribution to journalComment/debate

22 Citations (Scopus)

Abstract

The Tax protein from human T-cell leukemia virus type I (HTLV-1) is a 40- kDa phosphoprotein capable of activating transcription from its own long terminal repeat (LTR), as well as increasing the transcription of cellular genes. Transcriptional activation of the HTLV-1 LTR has been demonstrated via a cyclic-AMP-responsive element within the 21-bp Tax-responsive elements of the LTR. Phorbol esters also upregulate expression via the LTR. Since phosphorylation of Tax may play a role in these processes, we investigated the relative effects of kinase-stimulating agents on 32P incorporation into Tax. Our studies demonstrated that the phorbol ester 4β-phorbol-12β- myristate-13α-acetate greatly stimulated Tax phosphorylation in a time- and dose-dependent manner. In contrast, 8-bromoadenosine 3'-5'-cyclic monophosphate induced little stimulation of Tax phosphorylation. Tax phosphorylation occurred only on serine residues and was mapped to a single tryptic fragment in both Tax-producing human lymphocytes and mouse fibroblast cells.

Original languageEnglish (US)
Pages (from-to)4436-4441
Number of pages6
JournalJournal of virology
Volume67
Issue number7
StatePublished - Jan 1 1993

Fingerprint

Primate T-lymphotropic virus 1
Human T-lymphotropic virus 1
Terminal Repeat Sequences
taxes
Phorbol Esters
phosphorylation
esters
Phosphorylation
terminal repeat sequences
Phosphoproteins
Cyclic AMP
Serine
Transcriptional Activation
transcription (genetics)
Acetates
Phosphotransferases
Up-Regulation
Fibroblasts
Lymphocytes
phosphoproteins

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Cite this

Phorbol esters modulate the phosphorylation of human T-cell leukemia virus type I Tax. / Fontes, Joseph D.; Strawhecker, Judith M.; Bills, Nathan D.; Lewis, Robert E; Hinrichs, Steven Heye.

In: Journal of virology, Vol. 67, No. 7, 01.01.1993, p. 4436-4441.

Research output: Contribution to journalComment/debate

Fontes, Joseph D. ; Strawhecker, Judith M. ; Bills, Nathan D. ; Lewis, Robert E ; Hinrichs, Steven Heye. / Phorbol esters modulate the phosphorylation of human T-cell leukemia virus type I Tax. In: Journal of virology. 1993 ; Vol. 67, No. 7. pp. 4436-4441.
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AU - Hinrichs, Steven Heye

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N2 - The Tax protein from human T-cell leukemia virus type I (HTLV-1) is a 40- kDa phosphoprotein capable of activating transcription from its own long terminal repeat (LTR), as well as increasing the transcription of cellular genes. Transcriptional activation of the HTLV-1 LTR has been demonstrated via a cyclic-AMP-responsive element within the 21-bp Tax-responsive elements of the LTR. Phorbol esters also upregulate expression via the LTR. Since phosphorylation of Tax may play a role in these processes, we investigated the relative effects of kinase-stimulating agents on 32P incorporation into Tax. Our studies demonstrated that the phorbol ester 4β-phorbol-12β- myristate-13α-acetate greatly stimulated Tax phosphorylation in a time- and dose-dependent manner. In contrast, 8-bromoadenosine 3'-5'-cyclic monophosphate induced little stimulation of Tax phosphorylation. Tax phosphorylation occurred only on serine residues and was mapped to a single tryptic fragment in both Tax-producing human lymphocytes and mouse fibroblast cells.

AB - The Tax protein from human T-cell leukemia virus type I (HTLV-1) is a 40- kDa phosphoprotein capable of activating transcription from its own long terminal repeat (LTR), as well as increasing the transcription of cellular genes. Transcriptional activation of the HTLV-1 LTR has been demonstrated via a cyclic-AMP-responsive element within the 21-bp Tax-responsive elements of the LTR. Phorbol esters also upregulate expression via the LTR. Since phosphorylation of Tax may play a role in these processes, we investigated the relative effects of kinase-stimulating agents on 32P incorporation into Tax. Our studies demonstrated that the phorbol ester 4β-phorbol-12β- myristate-13α-acetate greatly stimulated Tax phosphorylation in a time- and dose-dependent manner. In contrast, 8-bromoadenosine 3'-5'-cyclic monophosphate induced little stimulation of Tax phosphorylation. Tax phosphorylation occurred only on serine residues and was mapped to a single tryptic fragment in both Tax-producing human lymphocytes and mouse fibroblast cells.

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