期刊
FEBS LETTERS
卷 589, 期 23, 页码 3508-3515出版社
WILEY
DOI: 10.1016/j.febslet.2015.10.018
关键词
Water channel; Osmotic permeability; Heteromerization
资金
- Prestamo BID [PICT11 2239]
- PIP [CONICET-1214]
- [UBACyT14-17]
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. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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