Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing
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...
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2016
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1858_n11_p2778_Yaneff http://hdl.handle.net/20.500.12110/paper_00052736_v1858_n11_p2778_Yaneff |
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paper:paper_00052736_v1858_n11_p2778_Yaneff2023-06-08T14:29:51Z Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing Sigaut, Lorena Gómez, Natalia Valeria 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 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. Fil:Sigaut, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gómez, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2016 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1858_n11_p2778_Yaneff http://hdl.handle.net/20.500.12110/paper_00052736_v1858_n11_p2778_Yaneff |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Sigaut, Lorena Gómez, Natalia Valeria Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing |
| topic_facet |
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 |
| description |
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. |
| author |
Sigaut, Lorena Gómez, Natalia Valeria |
| author_facet |
Sigaut, Lorena Gómez, Natalia Valeria |
| author_sort |
Sigaut, Lorena |
| title |
Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing |
| title_short |
Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing |
| title_full |
Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing |
| title_fullStr |
Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing |
| title_full_unstemmed |
Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing |
| title_sort |
loop b serine of a plasma membrane aquaporin type pip2 but not pip1 plays a key role in ph sensing |
| publishDate |
2016 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1858_n11_p2778_Yaneff http://hdl.handle.net/20.500.12110/paper_00052736_v1858_n11_p2778_Yaneff |
| work_keys_str_mv |
AT sigautlorena loopbserineofaplasmamembraneaquaporintypepip2butnotpip1playsakeyroleinphsensing AT gomeznataliavaleria loopbserineofaplasmamembraneaquaporintypepip2butnotpip1playsakeyroleinphsensing |
| _version_ |
1768542484784218112 |