INVESTIGADORES
ANGEL Sergio Oscar
artículos
Título:
Protozoan HSP90-Heterocomplex: Molecular Interaction Network and Biological Significance.
Autor/es:
FIGUERAS MJ; ECHEVERIA PC; ANGEL SO
Revista:
CURRENT PROTEIN AND PEPTIDE SCIENCE
Editorial:
BENTHAM SCIENCE PUBL LTD
Referencias:
Lugar: Oak Park; Año: 2014
ISSN:
1389-2037
Resumen:
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.