Polo-box domain: a versatile mediator of polo-like kinase function

Cell Mol Life Sci. 2010 Jun;67(12):1957-70. doi: 10.1007/s00018-010-0279-9. Epub 2010 Feb 11.

Abstract

Members of the polo subfamily of protein kinases have emerged as important regulators in diverse aspects of the cell cycle and cell proliferation. A large body of evidence suggests that a highly conserved polo-box domain (PBD) present in the C-terminal non-catalytic region of polo kinases plays a pivotal role in the function of these enzymes. Recent advances in our comprehension of the mechanisms underlying mammalian polo-like kinase 1 (Plk1)-dependent protein-protein interactions revealed that the PBD serves as an essential molecular mediator that brings the kinase domain of Plk1 into proximity with its substrates, mainly through phospho-dependent interactions with its target proteins. In this review, current understanding of the structure and functions of PBD, mode of PBD-dependent interactions and substrate phosphorylation, and other phospho-independent functions of PBD are discussed.

Publication types

  • Review

MeSH terms

  • Cell Cycle Proteins / chemistry*
  • Cell Cycle Proteins / metabolism
  • Humans
  • Phosphorylation
  • Protein Kinases / chemistry*
  • Protein Kinases / metabolism
  • Protein-Serine-Threonine Kinases / chemistry*
  • Protein-Serine-Threonine Kinases / metabolism
  • Proto-Oncogene Proteins / chemistry*
  • Proto-Oncogene Proteins / metabolism

Substances

  • Cell Cycle Proteins
  • Proto-Oncogene Proteins
  • Protein Kinases
  • Protein-Serine-Threonine Kinases
  • polo-like kinase 1