INVESTIGADORES
TOUZ Maria Carolina
congresos y reuniones científicas
Título:
Vacuolar protein sorting receptor: new molecular evidence of a sorting pathway in Giardia lamblia.
Autor/es:
MIRAS S; RIVERO MR; FELIZIANI C; ZAMPONI N; QUIROGA R; ROPOLO AS; TOUZ MC
Lugar:
Mendoza
Reunión:
Congreso; SAIB; 2012
Resumen:
In , lysosome-like peripheral vacuoles (PVs) need to
specifically coordinate their endosomal and lysosomal functions to
be able to successfully perform endocytosis, protein degradation and
protein delivery, but how cargo, ligands and molecular components
generate specific routes to the PVs remains poorly understood.
Recently, we found that delivering membrane Cathepsin C and the
soluble acid phosphatase (AcPh) to the PVs is adaptin (AP1)-
dependent. However, the receptor that links AcPh and AP1 was
never described.We have studied protein-binding to AcPh by using
H6-taggedAcPh, and found that a membrane protein interacted with
AcPh. This protein, named GlVps (for Giardia lamblia Vacuolar
protein sorting), mainly localized to the ER-nuclear envelope and in
some PVs, probably function as the sorting receptor for AcPh. The
tyrosine-binding motif found in the C-terminal cytoplasmic tail
domain of GlVps was essential for its exit from the endoplasmic
reticulum and transport to the vacuoles, with this motif being
necessary for the interaction with the medium subunit of AP1. Thus,
the mechanism by which soluble proteins, such as AcPh, reach the
peripheral vacuoles in appears to be very similar to the
mechanism of lysosomal protein-sorting in more evolved eukaryotic
cells.