Artículo

Yaneff, A.; Sigaut, L.; Gómez, N.; Aliaga Fandiño, C.; Alleva, K.; Pietrasanta, L.I.; Amodeo, G. "Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing" (2016) Biochimica et Biophysica Acta - Biomembranes. 1858(11):2778-2787
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Abstract:

In the plant kingdom, the plasma membrane intrinsic aquaporins (PIPs) constitute a highly conserved group of water channels with the capacity of rapidly adjusting the water permeability (Pf) of a cell by a gating response. Most evidence regarding this mechanism was obtained by different biophysical approaches including the crystallization of a Spinaca olaracea PIP2 aquaporin (SoPIP2;1) in an open and close conformation. A close state seems to prevail under certain stimuli such as cytosolic pH decrease, intracellular Ca2 + concentration increase and dephosphorylation of specific serines. In this work we decided to address whether the state of phosphorylation of a loop B serine - highly conserved in all PIPs - combined with cytosolic acidification can jointly affect the gating response. To achieve this goal we generated loop B serine mutants of two PIP types of Fragaria × ananassa (FaPIP2;1S121A and FaPIP1;1S131A) in order to simulate a dephosphorylated state and characterize their behavior in terms of Pf and pH sensitivities. The response was tested for different co-expressions of PIPs (homo and heterotetramers combining wild-type and mutant PIPs) in Xenopus oocytes. Our results show that loop B serine phosphorylation status affects pH gating of FaPIP2;1 but not of FaPIP1;1 by changing its sensitivity to more alkaline pHs. Therefore, we propose that a counterpoint of different regulatory mechanisms - heterotetramerization, serine phosphorylation status and pH sensitivity - affect aquaporin gating thus ruling the Pf of a membrane that expresses PIPs when fast responses are mandatory. © 2016 Elsevier B.V.

Registro:

Documento: Artículo
Título:Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing
Autor:Yaneff, A.; Sigaut, L.; Gómez, N.; Aliaga Fandiño, C.; Alleva, K.; Pietrasanta, L.I.; Amodeo, G.
Filiación:Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Instituto de Biodiversidad y Biología Experimental (IBBEA, UBA-CONICET), Buenos Aires, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires, Argentina
Departamento de Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Instituto de Física de Buenos Aires, (IFIBA, UBA-CONICET), Buenos Aires, Argentina
Centro de Microscopías Avanzadas (CMA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Instituto de Investigaciones Farmacológicas (ININFA), Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave:Aquaporin gating; Cytosolic acidification; Heteromerization; Osmotic permeability; Water channel; Water transport; aquaporin; aquaporin type PIP1; aquaporin type PIP2; serine; unclassified drug; aquaporin; plant protein; recombinant protein; serine; water; acidification; alkalinity; animal cell; Article; calcium cell level; channel gating; controlled study; crystallization; dephosphorylation; Fragaria; nonhuman; oocyte; pH; priority journal; protein conformation; spinach; water permeability; Xenopus; Ananas; animal; cell membrane; chemistry; gene expression; genetics; kinetics; metabolism; mutation; pH; phosphorylation; protein multimerization; protein secondary structure; signal transduction; Ananas; Animals; Aquaporins; Cell Membrane; Fragaria; Gene Expression; Hydrogen-Ion Concentration; Kinetics; Mutation; Oocytes; Phosphorylation; Plant Proteins; Protein Multimerization; Protein Structure, Secondary; Recombinant Proteins; Serine; Signal Transduction; Water; Xenopus
Año:2016
Volumen:1858
Número:11
Página de inicio:2778
Página de fin:2787
DOI: http://dx.doi.org/10.1016/j.bbamem.2016.08.002
Título revista:Biochimica et Biophysica Acta - Biomembranes
Título revista abreviado:Biochim. Biophys. Acta Biomembr.
ISSN:00052736
CODEN:BBBMB
CAS:aquaporin, 215587-75-0; serine, 56-45-1, 6898-95-9; water, 7732-18-5; Aquaporins; Plant Proteins; Recombinant Proteins; Serine; Water
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1858_n11_p2778_Yaneff

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Citas:

---------- APA ----------
Yaneff, A., Sigaut, L., Gómez, N., Aliaga Fandiño, C., Alleva, K., Pietrasanta, L.I. & Amodeo, G. (2016) . Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing. Biochimica et Biophysica Acta - Biomembranes, 1858(11), 2778-2787.
http://dx.doi.org/10.1016/j.bbamem.2016.08.002
---------- CHICAGO ----------
Yaneff, A., Sigaut, L., Gómez, N., Aliaga Fandiño, C., Alleva, K., Pietrasanta, L.I., et al. "Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing" . Biochimica et Biophysica Acta - Biomembranes 1858, no. 11 (2016) : 2778-2787.
http://dx.doi.org/10.1016/j.bbamem.2016.08.002
---------- MLA ----------
Yaneff, A., Sigaut, L., Gómez, N., Aliaga Fandiño, C., Alleva, K., Pietrasanta, L.I., et al. "Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing" . Biochimica et Biophysica Acta - Biomembranes, vol. 1858, no. 11, 2016, pp. 2778-2787.
http://dx.doi.org/10.1016/j.bbamem.2016.08.002
---------- VANCOUVER ----------
Yaneff, A., Sigaut, L., Gómez, N., Aliaga Fandiño, C., Alleva, K., Pietrasanta, L.I., et al. Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing. Biochim. Biophys. Acta Biomembr. 2016;1858(11):2778-2787.
http://dx.doi.org/10.1016/j.bbamem.2016.08.002