Activated NLK phosphorylates TCF7L2 and LEF1 at serine and threonine residues that lie in the central region between the DNA-binding and beta-catenin interaction domains. Phosphorylation does not affect the ability of TCF/LEF to bind to beta-catenin, but the phosphorylated complex is not able to bind to target DNA or activate transcription as assessed by EMSA and reporter gene assays (Ishitani et al, 2003b).
Ishitani, T, Matsumoto, K, Ninomiya-Tsuji, J
protein serine/threonine kinase activity of pT298-NLK dimer [nucleoplasm]
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