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

Trends Biochem Sci. 1993 Sep;18(9):343-8. doi: 10.1016/0968-0004(93)90071-t.


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 beta-adrenergic receptor kinase exactly in the region that has already been shown to be involved in binding to the beta and gamma subunits of a heterotrimeric G protein. This suggests that PH domains may be involved in interactions with GTP-binding proteins.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blood Proteins / chemistry*
  • Blood Proteins / metabolism
  • GTP-Binding Proteins / metabolism
  • Humans
  • Molecular Sequence Data
  • Phosphoproteins*
  • Sequence Homology, Amino Acid
  • Signal Transduction


  • Blood Proteins
  • Phosphoproteins
  • platelet protein P47
  • GTP-Binding Proteins