Identification of a functional destruction box in the Xenopus laevis aurora-A kinase pEg2

FEBS Lett. 2001 Nov 9;508(1):149-52. doi: 10.1016/s0014-5793(01)03048-4.

Abstract

Like for all aurora-A kinases, the Xenopus pEg2 kinase level peaks in G(2)/M and is hardly detectable in G(1) cells, suggesting that the protein is degraded upon exit from mitosis as reported for the human aurora-A kinase. We identified for the first time a sequence RxxL in the C-terminal end of the kinase catalytic domain. Mutation of this sequence RxxL to RxxI suppresses the ubiquitination of the protein as well as its degradation. The sequence RxxL corresponding to the pEg2 functional destruction box has been conserved throughout evolution in all aurora kinases including aurora-A, -B and -C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Aurora Kinases
  • Catalytic Domain
  • Cell Cycle Proteins / chemistry*
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism
  • Humans
  • Molecular Sequence Data
  • Point Mutation
  • Protein Kinases / chemistry*
  • Protein Kinases / genetics*
  • Protein Kinases / metabolism
  • Protein-Serine-Threonine Kinases
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Ubiquitin / metabolism
  • Xenopus Proteins
  • Xenopus laevis

Substances

  • Cell Cycle Proteins
  • Recombinant Proteins
  • Ubiquitin
  • Xenopus Proteins
  • Protein Kinases
  • AURKA protein, Xenopus
  • Aurora Kinases
  • Protein-Serine-Threonine Kinases