The PH domain: a common piece in the structural pathcwork of signalling proteins

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Abstract

The ‘pleckstrin homology’ domain is an approximately 100-residue protein module that has recently been added to the domain catalogue of signalling proteins. For this review we have made an extensive database search using a profile search method, and found a number of additional proteins that may contain PH domains. The PH domain is present in many kinases, isoforms of phospholipase C, GTPases, GTPase-activating proteins and nucleotide-exchange factors, including such proteins as Vav, Dbl and Bcr, and there are two PH domains in a guanine-nucleotide releasing factor of Ras. Many PH-domain-containing proteins interact with GTP-binding proteins. We have also identified a PH domain in β-adrenergic receptor kinase exactly in the region that has already been shown to be involved in binding to the β and γ subunits of a heterotrimeric G protein. This suggests that PH domains may be involved in interactions with GTP-binding proteins.

References (44)

  • B.J. Mayer et al.

    Cell

    (1993)
  • T. Pawson et al.

    Cell

    (1992)
  • A. Musacchio et al.

    FEBS Lett.

    (1992)
  • G.W. Booker

    Cell

    (1993)
  • J.P. Olivier

    Cell

    (1993)
  • W.R. Taylor

    J. Mol. Biol.

    (1986)
  • T.J. Gibson et al.

    FEBS Lett.

    (1993)
  • S. Miyamoto et al.

    Gene

    (1987)
  • Y. Maru et al.

    Cell

    (1991)
  • R.B. Russell et al.

    FEBS Lett.

    (1992)
  • W.J. Koch et al.

    J. Biol. Chem.

    (1993)
  • R.J. Haslam et al.

    Nature

    (1993)
  • M. Tyers

    Nature

    (1988)
  • M. Trahey

    Science

    (1988)
  • C. Shou et al.

    Nature

    (1992)
  • M.I. Simon et al.

    Science

    (1991)
  • A. Bellacosa et al.

    Science

    (1991)
  • P.F. Jones
  • B. Margolis
  • P. Cicchetti et al.

    Science

    (1992)
  • R. Ren et al.

    Science

    (1993)
  • S.E. Egan

    Nature

    (1993)
  • Cited by (0)

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