Ser119 phosphorylation modulates the activity and conformation of PRRXL1, a homeodomain transcription factor

In this study, we show that PRRXL1 is highly phosphorylated in vivo, and that its multiple band pattern on electrophoretic analysis is the result of different phosphorylation states. PRRXL1 phosphorylation appears to be differentially regulated along the dSC and DRG development and it is mapped to two functional domains. One region comprises amino acids 107-143, while the other one encompasses amino acids 227-263 and displays repressor activity. Using an immunoprecipitation-MS approach, two phosphorylation sites were identified: S119 and S238. Phosphorylation at S119 is shown to be determinant for PRRXL1 conformation and transcriptional activity. S119 phosphorylation is thus proposed as a mechanism for regulating PRRXL1 function and conformation during nociceptive system development.

Source: BJ Gene - February 24, 2014 Category: Biochemistry Authors: R Soares-dos-Reis, A Sofia Pessoa, M Raimundo Matos, M Falcão, V M Mendes, B Manadas, F Almeida Monteiro, D Lima, C Reguenga Tags: BJ Biomolecules Source Type: research