Histone deacetylase 8 interacts with the GTPase SmRho1 in Schistosoma mansoni

International audienceSchistosoma mansoni histone deacetylase 8 (SmHDAC8) has elicited considerable interestas a target for drug discovery. Invalidation of its transcripts by RNAi leads to impaired survivalof the worms in infected mice and its inhibition causes cell apoptosis and death. Todetermine why it is a promising therapeutic target the study of the currently unknown cellularsignaling pathways involving this enzyme is essential. Protein partners of SmHDAC8 werepreviously identified by yeast two-hybrid (Y2H) cDNA library screening and by mass spectrometry(MS) analysis. Among these partners we characterized SmRho1, the schistosomeorthologue of human RhoA GTPase, which is involved in the regulation of the cytoskeleton.In this work, we validated the interaction between SmHDAC8 and SmRho1 and exploredthe role of the lysine deacetylase in cytoskeletal regulation