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Mutational analysis of two residues in the DYRK homology box of the protein kinase DYRK1A.

Esti Wahyu WidowatiSimone Bamberg-LemperWalter Becker
Published in: BMC research notes (2018)
When expressed in HeLa cells, DYRK1A-D138P and K150C showed no significant difference from wild type DYRK1A regarding the activating tyrosine autophosphorylation or catalytic activity towards exogenous substrates. However, both DYRK1A variants were underphosphorylated on tyrosine when expressed in a bacterial cell free in vitro translation system. These results suggest that D138 and K150 participate in the maturation of the catalytic domain of DYRK1A albeit the mutation of these residues is compensated under physiological conditions.
Keyphrases
  • cell free
  • wild type
  • induced apoptosis
  • cell cycle arrest
  • protein kinase
  • transcription factor
  • signaling pathway
  • gene expression
  • cell death
  • copy number
  • oxidative stress
  • circulating tumor
  • circulating tumor cells