Splicing factors have recently been shown to be involved in heterochromatin formation, but their role in controlling heterochromatin structure and function remains poorly understood. In this study, we identified a fission yeast homologue of human splicing factor RBM10, which has been linked to TARP syndrome. Overexpression of Rbm10 in fission yeast leads to strong global intron retention. Rbm10 also interacts with splicing factors in a pattern resembling that of human RBM10, suggesting that the function of Rbm10 as a splicing regulator is conserved. Surprisingly, our deep-sequencing data showed that deletion of Rbm10 caused only minor effect on genome-wide gene expression and splicing. However, the mutant displays severe heterochromatin defects. Further analyses confirmed that the heterochromatin defects in the mutant did not result from mis-splicing of heterochromatin factors. Our proteomic data revealed that Rbm10 associates with the histone deacetylase Clr6 complex and chromatin remodeling complexes known to be essential for heterochromatin silencing. We propose that Rbm10 serves as a platform to recruit Clr6 and chromatin remodelers to mediate heterochromatin formation. Our work together with previous findings further suggests that different splicing subunits may play distinct roles in heterochromatin regulation. Overall design: Poly (A) RNA was prepared from total RNA by two rounds of oligo (dT)25 Dynabeads (Invitrogen) purification. Following fragmentation at 94°C for 3.5 min, the RNA was converted to first strand cDNA using random hexmer primer and Supescript II (Invitrogen), followed by second strand cDNA synthesis with Eschericcia coli DNA pol I (Invitrogen) and RNAse H (Invitrogen). The barcoded sequencing library was prepared and sequenced on Illumina HiSeq for 1 × 100 cycles following the standard protocol.