Yaneff, A.; Sigaut, L.; Marquez, M.; Alleva, K.; Pietrasanta, L.I.; Amodeo, G. "Heteromerization of PIP aquaporins affects their intrinsic permeability" (2014) Proceedings of the National Academy of Sciences of the United States of America. 111(1):231-236
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The plant aquaporin plasma membrane intrinsic proteins (PIP) subfamily represents one of the main gateways for water exchange at the plasma membrane (PM). A fraction of this subfamily, known as PIP1, does not reach the PM unless they are coexpressed with a PIP2 aquaporin. Although ubiquitous and abundantly expressed, the role and properties of PIP1 aquaporins have therefore remained masked. Here, we unravel how FaPIP1;1, a fruit-specific PIP1 aquaporin from Fragaria x ananassa, contributes to the modulation of membrane water permeability (Pf) and pH aquaporin regulation. Our approach was to combine an experimental and mathematical model design to test its activity without affecting its trafficking dynamics. We demonstrate that FaPIP1;1 has a high water channel activity when coexpressed as well as how PIP1-PIP2 affects gating sensitivity in terms of cytosolic acidification. PIP1-PIP2 random heterotetramerization not only allows FaPIP1;1 to arrive at the PMbut also produces an enhancement of FaPIP2;1 activity. In this context, we propose that FaPIP1;1 is a key participant in the regulation of water movement across the membranes of cells expressing both aquaporins.


Documento: Artículo
Título:Heteromerization of PIP aquaporins affects their intrinsic permeability
Autor:Yaneff, A.; Sigaut, L.; Marquez, M.; Alleva, K.; Pietrasanta, L.I.; Amodeo, G.
Filiación:Instituto de Biodiversidad y Biología Experimental, Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, C1428EHA Buenos Aires, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas, Argentina
Centro de Microscopías Avanzadas, Departamento de Física, Facultad de Ciencias Exactas y Naturales, C1428EHA Buenos Aires, Argentina
Palabras clave:aquaporin; membrane protein; plasma membrane intrinsic protein 1; plasma membrane intrinsic protein 2; unclassified drug; acidification; article; cell membrane; channel gating; mathematical model; membrane permeability; molecular dynamics; permeability; pH; priority journal; protein expression; protein function; protein interaction; protein transport; regulatory mechanism; strawberry; water flow; water permeability; Animals; Aquaporins; Bacterial Proteins; Cell Membrane; Cytosol; Fragaria; Gene Expression Regulation, Plant; Hydrogen-Ion Concentration; Lipid Bilayers; Luminescent Proteins; Microscopy, Confocal; Models, Theoretical; Mutagenesis, Site-Directed; Oocytes; Permeability; Plant Proteins; Protein Multimerization; RNA, Complementary; Water; Xenopus laevis
Página de inicio:231
Página de fin:236
Título revista:Proceedings of the National Academy of Sciences of the United States of America
Título revista abreviado:Proc. Natl. Acad. Sci. U. S. A.
CAS:aquaporin, 215587-75-0


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---------- APA ----------
Yaneff, A., Sigaut, L., Marquez, M., Alleva, K., Pietrasanta, L.I. & Amodeo, G. (2014) . Heteromerization of PIP aquaporins affects their intrinsic permeability. Proceedings of the National Academy of Sciences of the United States of America, 111(1), 231-236.
---------- CHICAGO ----------
Yaneff, A., Sigaut, L., Marquez, M., Alleva, K., Pietrasanta, L.I., Amodeo, G. "Heteromerization of PIP aquaporins affects their intrinsic permeability" . Proceedings of the National Academy of Sciences of the United States of America 111, no. 1 (2014) : 231-236.
---------- MLA ----------
Yaneff, A., Sigaut, L., Marquez, M., Alleva, K., Pietrasanta, L.I., Amodeo, G. "Heteromerization of PIP aquaporins affects their intrinsic permeability" . Proceedings of the National Academy of Sciences of the United States of America, vol. 111, no. 1, 2014, pp. 231-236.
---------- VANCOUVER ----------
Yaneff, A., Sigaut, L., Marquez, M., Alleva, K., Pietrasanta, L.I., Amodeo, G. Heteromerization of PIP aquaporins affects their intrinsic permeability. Proc. Natl. Acad. Sci. U. S. A. 2014;111(1):231-236.