IBBEA   24401
INSTITUTO DE BIODIVERSIDAD Y BIOLOGIA EXPERIMENTAL Y APLICADA
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Aquaporin Trafficking as a Specific Regulatory Mechanism to Adjust Membrane Water Permeability
Autor/es:
GABRIELA AMODEO, YANEFF AGUSTIN, JOZEFKOWICZ CINTIA, MARQUEZ MERCEDES, VITALI VICTORIA, SCOCHERA FLORENCIA, ALLEVA KARINA
Lugar:
San Francisco
Reunión:
Congreso; 58th Annual Meeting Biophysical Society; 2014
Institución organizadora:
Biophysical Society
Resumen:
Aquaporin Trafficking as a Specific Regulatory Mechanism to Adjust Membrane Water Permeability Gabriela Amodeo, Yaneff Agustin, Jozefkowicz Cintia, Marquez Mercedes, Vitali Victoria, Scochera Florencia and Alleva Karina IBBEA DBBE, Universidad de Buenos Aires, Buenos Aires, Argentina Plant aquaporins regulate water fluxes across membranes by enhancing membrane water permeability (Pf). In particular, the plant plasma membrane holds PIPs, one of the largest groups of aquaporins. PIPs are divided in two clusters (PIP1 and PIP2) that disclose intriguing aspects: i) the potential of modulating Pf by PIP1-PIP2 co-expression, distinguished for each PIP showing differential capacity to reach the PM and ii), the faculty to reduce water permeation through the pore after cytosolic acidification, as a consequence of a gating process. Our working hypothesis is that cytosolic pH (gating) and PIP co-expression (trafficking) enhance plasticity to the membrane water transport capacity as a consequence of a PIP1-PIP2 cooperative interaction. Thus, PIP1 cellular trafficking and its effect in water permeability emerge as playing a key role as a regulatory mechanism. To analyze this interaction we used PIP1-PIP2 pairs from different species (Fragaria ananassa and Beta vulgaris). Our experimental approach included i) designing mutants to alter the PIP-PIP2 interaction by means of site directed mutagenesis; ii) tracking aquaporin localization -at internal structures or expressed at the level of the PM-; and iii) analyzing water transport capacity in control and inhibited (medium acidification) conditions by means of measuring Pf in Xenopus oocytes. Our finding support evidences in agreement with the concept that PIP2 and PIP1 interact to form functional heterooligomeric assemblies, and thus the composition of these PIP assemblies determines their functional properties. As PIP1 alone is not able to reach the plasma membrane its contribution to enhance water permeability is associated to its translocation and interaction with a PIP2. This regulatory mechanism seems to be present in different vascular plants. This information is integrated in a proposal for water transport pathways including the organs where this PIPs are present. 2820-PosB512