INVESTIGADORES
AYUB Nicolas Daniel
congresos y reuniones científicas
Título:
Functional and structural characterization of three different PIP aquaporins
Autor/es:
SCOCHERA F; JOSEF C; SOTO G; AYUB ND; AMODEO G; ALLEVA K
Lugar:
Cordoba
Reunión:
Congreso; SAB; 2013
Institución organizadora:
SAB
Resumen:
Among plant aquaporins, three subfamilies
are involved in the modulation of the permeability of the plasma membrane (NIP,
XIP and PIP). Within these, only PIP are known for their capacity to form
heteromeric complexes by the interaction of different members of the subfamily.
PIP members are usually known as PIP1 and PIP2, but we recently showed that
they are better described as three PIP-like clusters instead of two: i- PIPCLI,
corresponding to the classical PIP1, ii- PIPCLII and iii- PIPCLIII, involving
most of PIP2 (1). ). It was shown that pairs of PIPs from different clusters
can interact. However, when expressed alone, important differences in
functionality of these channels was addressed (2, 3). With the aim of exploring
how these three clusters can provide us information regarding these
interactions, we analyzed the functional and structural profile of three Beta vulgaris PIP, one corresponding to
each cluster, BvPIP2;1 (PIPCLIII), BvPIP1;1 (PIPCLI) and BvPIP2;2 (PIPCLII). We
compare their water and solute transport activity, inhibition, and molecular
structures. The dissection of each channel particularities is a key tool to
understand their participation in the functionality not only of
homomeric complexes but also when assembling as heterotetramers.