Identification of a functional destruction box in the Xenopus laevis aurora-A kinase pEg2.
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.
Arlot-Bonnemains
Y
Y
Groupe Cycle Cellulaire, UMR 6061 Génétique et Développement, CNRS-Université de Rennes 1, IFR 97 Génomique Fonctionnelle et Santé, Faculté de Médecine, 2 avenue du Pr Léon Bernard, CS 34317, 35043 Rennes Cedex, France. yannick.arlot@univ-rennes1.fr
Klotzbucher
A
A
Giet
R
R
Uzbekov
R
R
Bihan
R
R
Prigent
C
C
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D064127:Aurora Kinases; D020134:Catalytic Domain; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D017354:Point Mutation; D011494:Protein Kinases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D025801:Ubiquitin / Q000378:metabolism; D029867:Xenopus Proteins; D014982:Xenopus laevis
D018797:Cell Cycle Proteins; D011994:Recombinant Proteins; D025801:Ubiquitin; D029867:Xenopus Proteins; D011494:Protein Kinases; C112134:AURKA protein, Xenopus; D064127:Aurora Kinases; D017346:Protein Serine-Threonine Kinases