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Tip60 acetyltransferase activity is controlled by phosphorylation.

Claudie Lemercier1, Gaëlle Legube, Cécile Caron

  • 1Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U309, Institut Albert Bonniot, Faculté de Médecine, Domaine de la Merci, 38706 La Tronche Cedex, France.

The Journal of Biological Chemistry
|December 7, 2002
PubMed
Summary
This summary is machine-generated.

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Phosphorylation of histone acetyltransferase Tip60, a target of HIV-1 Tat, regulates its activity. This G(2)/M-dependent process involves specific phosphorylation sites identified via mass spectrometry.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Cycle Regulation

Background:

  • Histone acetyltransferase Tip60 is a target of the human immunodeficiency virus type 1 (HIV-1) transactivator Tat.
  • Tip60's catalytic activity is crucial for various cellular processes.

Purpose of the Study:

  • To investigate the role of Tip60 phosphorylation in controlling its catalytic activity.
  • To identify specific phosphorylation sites on Tip60 and their regulatory mechanisms.

Main Methods:

  • Baculovirus-based expression and purification of Tip60.
  • Mass spectrometry for identification of phosphorylation sites.
  • In vitro kinase assays using cyclin B/Cdc2 complex.
  • Cell cycle arrest studies (G(2)/M) and inhibitor treatments (roscovitine).

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Main Results:

  • Serines 86 and 90 were identified as major in vivo phosphorylation sites on Tip60.
  • Tip60 phosphorylation modulates its histone acetyltransferase activity.
  • Serine-90 is a cyclin B/Cdc2 phosphorylation site, with Tip60 phosphorylation enhanced in G(2)/M phase and inhibited by roscovitine.

Conclusions:

  • Tip60 activity is regulated by phosphorylation.
  • A G(2)/M-dependent mechanism controls Tip60 activity through cyclin B/Cdc2-mediated phosphorylation.
  • Understanding Tip60 regulation offers insights into HIV-1 interactions and cell cycle control.