Histone deacetylase 8 interacts with the GTPase SmRho1 in Schistosoma mansoni.
Lucile PagliazzoStéphanie CabyJulien LancelotSophie Salome-DesnoulezJean Michel SaliouTino HeimburgThierry ChassatKatia CailliauWolfgang SipplJérôme VicogneRaymond J PiercePublished in: PLoS neglected tropical diseases (2021)
Our results suggest that SmHDAC8 is involved in cytoskeleton organization via its interaction with the SmRho1.1 isoform. The SmRho1.2 isoform failed to interact with SmHDAC8, but did specifically interact with SmDia suggesting the existence of two distinct signaling pathways regulating S. mansoni cytoskeleton organization via the two SmRho1 isoforms. A specific interaction between SmHDAC8 and the C-terminal moiety of SmRho1.1 was demonstrated, and we showed that SmRho1 is acetylated on K136. SmHDAC8 inhibition or knockdown using RNAi caused extensive disruption of schistosomula actin cytoskeleton.