INVESTIGADORES
PARUSSINI GIMENEZ Silvana Fabiola
artículos
Título:
Cathepsin L occupies a vacuolar compartment and is a protein maturase within the endo/exocytic system of Toxoplasma gondii
Autor/es:
FABIOLA PARUSSINI; ISABELLE COPPENS; PARAG P. SHAH ; SCOTT L. DIAMOND; VERN B. CARRUTHERS
Revista:
MOLECULAR MICROBIOLOGY
Editorial:
WILEY-BLACKWELL PUBLISHING, INC
Referencias:
Lugar: Londres; Año: 2010 vol. 76 p. 1340 - 1357
ISSN:
0950-382X
Resumen:
Regulated exocytosis allows the timely delivery of proteins and other
macromolecules precisely when they are needed to fulfill their
functions. The intracellular parasite Toxoplasma gondii has one
of the most extensive regulated exocytic systems among all unicellular
organisms, yet the basis of protein trafficking and proteolytic
modification in this system is poorly understood. We demonstrate that a
parasite cathepsin protease, TgCPL, occupies a newly recognized vacuolar compartment (VAC) that undergoes dynamic fragmentation during T. gondii
replication. We also provide evidence that within the VAC or late
endosome this protease mediates the proteolytic maturation of
proproteins targeted to micronemes, regulated secretory organelles that
deliver adhesive proteins to the parasite surface during cell invasion.
Our findings suggest that processing of microneme precursors occurs
within intermediate endocytic compartments within the exocytic system,
indicating an extensive convergence of the endocytic and exocytic
pathways in this human parasite.