SRSF10 (also known as SRp38) is a splicing factor that acts as a potent and general splicing repressor when dephosphorylated [, , ]. It mediates global inhibition of splicing both in M phase of the cell cycle and in response to heat shock [, ]. SRSF10 emerges as a modulator of cholesterol homeostasis through the regulation of low-density lipoprotein receptor (LDLR) splicing efficiency []. It regulates cardiac-specific alternative splicing of triadin pre-mRNA and is required for proper Ca2+ handling during embryonic heart development []. In contrast, the phosphorylated SRSF10 functions as a sequence-specific splicing activator in the presence of a nuclear cofactor. It activates distal alternative 5' splice site of adenovirus E1A pre-mRNA in vivo. Moreover, SRSF10 strengthens pre-mRNA recognition by U1 and U2 snRNPs []. It contains a single N-terminal RNA recognition motif (RRM), followed by a C-terminal RS domain rich in serine-arginine dipeptides [].
