Histone deacetylase 8 interacts with the GTPase SmRho1 in Schistosoma mansoni
Abstract
Schistosoma mansoni histone deacetylase 8 (SmHDAC8) has elicited considerable interest
as a target for drug discovery. Invalidation of its transcripts by RNAi leads to impaired survival
of the worms in infected mice and its inhibition causes cell apoptosis and death. To
determine why it is a promising therapeutic target the study of the currently unknown cellular
signaling pathways involving this enzyme is essential. Protein partners of SmHDAC8 were
previously identified by yeast two-hybrid (Y2H) cDNA library screening and by mass spectrometry
(MS) analysis. Among these partners we characterized SmRho1, the schistosome
orthologue 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 explored
the role of the lysine deacetylase in cytoskeletal regulation.
Domains
Animal biology
Origin : Publisher files allowed on an open archive