IBBEA   24401
INSTITUTO DE BIODIVERSIDAD Y BIOLOGIA EXPERIMENTAL Y APLICADA
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Functional and structural characterization of three different PIP aquaporins
Autor/es:
FLORENCIA SCOCHERA; CINTIA JOZEFKOWICZ; GABRIELA SOTO; NICOLAS AYUB; GABRIELA AMODEO; KARINA ALLEVA
Lugar:
Carlos Paz
Reunión:
Congreso; XLII Reunión Anual de la Sociedad Argentina de Biofisica; 2013
Institución organizadora:
Sociedad Argentina de Biofisica
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.