The expression of Welander distal myopathy-related TIA1 mutation exacerbates the dynamics of P-bodies and stress granules under oxidative stress

T-cell intracellular antigen 1 (TIA1) is an RNA-binding protein that is primarily involved in the post-transcriptional control of the cellular fate of RNAs. Moreover, it is a key component of stress granules (SGs), RNA and protein aggregates that are formed in response to stressful stimuli to reduce cellular activity as a survival mechanism. TIA1 p.E384K mutation is the genetic cause of Welander distal myopathy (WDM), a late-onset muscular dystrophy whose pathogenesis has been related to modify SGs dynamics. In this study, we have focused on the differential transcriptomic and proteomic characterization of purified wild-type (WT) and WDM TIA1-dependent SGs by affinity immunopurification followed by mass spectrometry and RNA seq analysis under oxidative stress. The results have revealed small differences in specific components of cellular machineries involving in regulating splicing, RNA degradation and/or translation linked to WDM TIA1 expression under oxidative stress. Our findings suggest a potential regulatory linking among WDM TIA1-dependent SGs and the number, size and colocalization/overlapping with P-bodies under oxidative stress. Taken together, these findings allow us to expand our knowledge on the role of Welander’s TIA1 mutation in interfacing SGs and P-bodies dynamics by involving potential regulatory impacts on cell machineries of RNA decay/turnover and/or translation.