Phosphorylation of SRSF1 at Tyr-19 promotes cell proliferation in pediatric acute lymphoblastic leukemia

we identified for the first time that the phosphorylation state of SRSF1 is linked to different phases in ALL. Our results underscore the phosphorylation of SRSF1 at the Tyr-19 residue disrupts subcellular localization of SRSF1 and promotes cell proliferation in leukemic cells by accelerating cell-cycle progression. Targeting Tie2 kinase is able to catalyze Tyr-19 phosphorylation of SRSF1, and offer a promising therapeutic target for the treatment of pediatric ALL. These findings undoubtedly add a new layer in understanding of how post-translational mechanism supports leukemia progression. Overall design: The mRNA profiles of stable leukemic cell line overexpressed wild-type SRSF1, mutants (SRSF1-Y19D or SRSF1-Y19F) or the empty vector were generated by deep sequencing using Illumina HiSeq 4000 platform