Molecular and Cellular Biochemistry

, Volume 227, Issue 1–2, pp 145–151 | Cite as

HIV-1 Rev transactivator: A β-subunit directed substrate and effector of protein kinase CK2

  • Flavio MeggioEmail author
  • Oriano Marin
  • Marco Boschetti
  • Stefania Sarno
  • Lorenzo A. Pinna


The phosphorylation of HIV-1 Rev by protein kinase CK2 is strictly dependent on the regulatory β subunit of the kinase and is deeply affected by conformational changes of the substrate outside the phosphorylation site [12]. Here we show that Rev modulates a variety of CK2 properties, including autophosphorylation, catalytic activity toward calmodulin, and susceptibility to polycationic effectors, whose common denominator is the involvement of the β subunit. Rev's two major CK2 sites are located at its N-terminus, immediately adjacent to a helix-loop-helix motif. By comparing the behaviour of full-size Rev with that of synthetic peptides reproducing, with suitable modifications, its N-terminal 26 amino acids including the phosphoacceptor site (Ser 5, Ser 8) and amphipathic helix-1, it appears that the functional interaction of the N-terminal portion of Rev with the N-terminal domain of the β subunit must rely on both electrostatic and hydrophobic interactions. The former mainly involve Rev's arginine-rich domain (residues 35–50) in helix-2, while the latter are mostly mediated by residues 12–24 of helix-1. These data disclose the possibility that, besides displaying protective, regulatory and targeting properties with respect to the catalytic subunit, the CK2 β subunit also plays a role as a docking site for a subset of CK2 substrates.

CK2 CKII casein kinase protein phosphorylation Rev 


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Copyright information

© Kluwer Academic Publishers 2001

Authors and Affiliations

  • Flavio Meggio
    • 1
    Email author
  • Oriano Marin
    • 2
  • Marco Boschetti
    • 2
  • Stefania Sarno
    • 1
  • Lorenzo A. Pinna
    • 2
  1. 1.Dipartimento di Chimica BiologicaPadovaItaly E-mail
  2. 2.Dipartimento di Chimica Biologica, Centro di Studio delle Biomembrane del CNR, and CRIBIUniversità di PadovaPadovaItaly

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