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PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators?
Author(s) -
Yaneff Agustín,
Vitali Victoria,
Amodeo Gabriela
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.10.018
Subject(s) - aquaporin , subfamily , microbiology and biotechnology , water channel , membrane , ion channel , membrane protein , aquaporin 1 , membrane channel , biology , chemistry , biophysics , biochemistry , receptor , gene , mechanical engineering , engineering , inlet
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.
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