Title:Protozoan HSP90-Heterocomplex: Molecular Interaction Network and Biological Significance
Volume: 15
Issue: 3
Author(s): Maria J. Figueras, Pablo C. Echeverria and Sergio O. Angel
Affiliation:
Keywords:
Co-chaperones, HSP90, network, Plasmodium, protein-protein interactors, Toxoplasma, trypanosomatids.
Abstract: The HSP90 chaperone is a highly conserved protein from bacteria to higher eukaryotes. In eukaryotes, this
chaperone participates in different large complexes, such as the HSP90 heterocomplex, which has important biological
roles in cell homeostasis and differentiation. The HSP90-heterocomplex is also named the HSP90/HSP70 cycle because
different co-chaperones (HIP, HSP40, HOP, p23, AHA1, immunophilins, PP5) participate in this complex by assembling
sequentially, from the early to the mature complex. In this review, we analyze the conservation and relevance of HSP90
and the HSP90-heterocomplex in several protozoan parasites, with emphasis in Plasmodium spp., Toxoplasma spp.,
Leishmania spp. and Trypanosoma spp. In the last years, there has been an outburst of studies based on yeast two-hybrid
methodology, co-immunoprecipitation-mass spectrometry and bioinformatics, which have generated a most comprehensive
protein-protein interaction (PPI) network of HSP90 and its co-chaperones. This review analyzes the existing PPI networks
of HSP90 and its co-chaperones of some protozoan parasites and discusses the usefulness of these powerful tools to
analyze the biological role of the HSP90-heterocomplex in these parasites. The generation of a T. gondii HSP90 heterocomplex
PPI network based on experimental data and a recent Plasmodium HSP90 heterocomplex PPI network are also
included and discussed. As an example, the putative implication of nuclear transport and chromatin (histones and Sir2) as
HSP90-heterocomplex interactors is here discussed.