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. 2011 Apr 15;25(8):801–813. doi: 10.1101/gad.2034211

Figure 3.

Figure 3.

DYRK1A interacts with LIN52 in vivo and phosphorylates LIN52-S28. (A) Positions and amino acid sequences of DYRK1A peptides detected in two independent LIN52 immunoprecipitation/MS-MS experiments. Dots indicate tryptic cleavage sites. (B) Clustal W alignment of DYRK1A orthologs from different species reveals a protein kinase family that is highly conserved in evolution. (C) Amino acid sequence around LIN52-S28 (black arrow), including the DYRK1A consensus motif (white arrows), is evolutionarily conserved. (D) In vitro kinase assay shows that both recombinant DYRK1A and DYRK1B can phosphorylate LIN52. Phosphorylated or total GST-LIN52 was detected by immunoblots with phospho-S28-LIN52 antibody and anti-GST antibody, respectively. (E) DYRK1A and DYRK1B were detected in BJ-hTERT and T98G cell extracts by immunoblot using recombinant purified GST-tagged proteins (rDYRK1A or rDYRK1B, 30 ng per lane) as a reference. The rDYRK1A and rDYRK1B samples were also blotted for GST to ensure equal loading.