PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators?
The highly conserved plant aquaporins, known as Plasma membrane Intrinsic Proteins (PIPs), are the main gateways for cell membrane water exchange. Years of research have described in detail the properties of the PIP2 subfamily. However, characterizing the PIP1 subfamily has been difficult due to the...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00145793_v589_n23_p3508_Yaneff |
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todo:paper_00145793_v589_n23_p3508_Yaneff2023-10-03T14:13:12Z PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators? Yaneff, A. Vitali, V. Amodeo, G. Heteromerization Osmotic permeability Water channel aquaporin plasma membrane Intrinsic protein 1 plasma membrane Intrinsic protein 2 unclassified drug aquaporin water nonhuman priority journal protein expression protein function protein interaction protein structure regulatory mechanism Review structure analysis water transport animal gene expression regulation metabolism transport at the cellular level Animals Aquaporins Biological Transport Gene Expression Regulation Water The highly conserved plant aquaporins, known as Plasma membrane Intrinsic Proteins (PIPs), are the main gateways for cell membrane water exchange. Years of research have described in detail the properties of the PIP2 subfamily. However, characterizing the PIP1 subfamily has been difficult due to the failure to localize to the plasma membrane. In addition, the discovery of the PIP1-PIP2 interaction suggested that PIP1 aquaporins could be regulated by a complex posttranslational mechanism that involves trafficking, heteromerization and fine-tuning of channel activity. This review not only considers the evidence and findings but also discusses the complexity of PIP aquaporins. To establish a new benchmark in PIP regulation, we propose to consider PIP1-PIP2 pairs as functional units for the purpose of future research into their physiological roles. © 2015 Federation of European Biochemical Societies. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00145793_v589_n23_p3508_Yaneff |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Heteromerization Osmotic permeability Water channel aquaporin plasma membrane Intrinsic protein 1 plasma membrane Intrinsic protein 2 unclassified drug aquaporin water nonhuman priority journal protein expression protein function protein interaction protein structure regulatory mechanism Review structure analysis water transport animal gene expression regulation metabolism transport at the cellular level Animals Aquaporins Biological Transport Gene Expression Regulation Water |
| spellingShingle |
Heteromerization Osmotic permeability Water channel aquaporin plasma membrane Intrinsic protein 1 plasma membrane Intrinsic protein 2 unclassified drug aquaporin water nonhuman priority journal protein expression protein function protein interaction protein structure regulatory mechanism Review structure analysis water transport animal gene expression regulation metabolism transport at the cellular level Animals Aquaporins Biological Transport Gene Expression Regulation Water Yaneff, A. Vitali, V. Amodeo, G. PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators? |
| topic_facet |
Heteromerization Osmotic permeability Water channel aquaporin plasma membrane Intrinsic protein 1 plasma membrane Intrinsic protein 2 unclassified drug aquaporin water nonhuman priority journal protein expression protein function protein interaction protein structure regulatory mechanism Review structure analysis water transport animal gene expression regulation metabolism transport at the cellular level Animals Aquaporins Biological Transport Gene Expression Regulation Water |
| description |
The highly conserved plant aquaporins, known as Plasma membrane Intrinsic Proteins (PIPs), are the main gateways for cell membrane water exchange. Years of research have described in detail the properties of the PIP2 subfamily. However, characterizing the PIP1 subfamily has been difficult due to the failure to localize to the plasma membrane. In addition, the discovery of the PIP1-PIP2 interaction suggested that PIP1 aquaporins could be regulated by a complex posttranslational mechanism that involves trafficking, heteromerization and fine-tuning of channel activity. This review not only considers the evidence and findings but also discusses the complexity of PIP aquaporins. To establish a new benchmark in PIP regulation, we propose to consider PIP1-PIP2 pairs as functional units for the purpose of future research into their physiological roles. © 2015 Federation of European Biochemical Societies. |
| format |
JOUR |
| author |
Yaneff, A. Vitali, V. Amodeo, G. |
| author_facet |
Yaneff, A. Vitali, V. Amodeo, G. |
| author_sort |
Yaneff, A. |
| title |
PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators? |
| title_short |
PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators? |
| title_full |
PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators? |
| title_fullStr |
PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators? |
| title_full_unstemmed |
PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators? |
| title_sort |
pip1 aquaporins: intrinsic water channels or pip2 aquaporin modulators? |
| url |
http://hdl.handle.net/20.500.12110/paper_00145793_v589_n23_p3508_Yaneff |
| work_keys_str_mv |
AT yaneffa pip1aquaporinsintrinsicwaterchannelsorpip2aquaporinmodulators AT vitaliv pip1aquaporinsintrinsicwaterchannelsorpip2aquaporinmodulators AT amodeog pip1aquaporinsintrinsicwaterchannelsorpip2aquaporinmodulators |
| _version_ |
1807317616796106752 |