Structural mechanism of plant aquaporin gating

By S. Törnroth-Horsefield, Yi Wang, Kristina Hedfalk, U. Johanson, M. Karlsson, Emad Tajkhorshid, R. Neutze, P. Kjellbom. Nature, 2006

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Water Flow in the Roots of Crop Species: The Influence of Root Structure, Aquaporin Activity, and Waterlogging (2007, background): “LoopD in PIPs is four to seven amino acid residues longer than other AQPs, which folds under the protein on the cytosolic side of the membrane and forms a cap occluding the cytosolic side of the pore (Törnroth-Horsefield et al., 2006, Section 5.3.3.1.1).”
Plant aquaporins: membrane channels with multiple integrated functions. (2008, background): “By contrast, phosphorylation of the C-terminal tail would act in trans to prevent loop D of an adjacent monomer from adopting a closed-pore conformation (137).”
PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update (2009, background): “More detailed studies have examined the roles of speciﬁc phosphorylation sites for the transport activities of aquaporins (8,9), the activity of the plasma membrane ATPase (10) and the regulation of speciﬁc metabolic enzymes by phosphorylation (11–13).”
Physiological roles of aquaporin-4 in brain. (2013, background): “The spinach plasma membrane aquaporin SoPIP2:1 is a case in point (188).”
Vacuolar transporters and their essential role in plant metabolism. (2006, background): “It has also been shown that some TIPs are regulated through phosphorylation (Maurel et al., 1995), as described for plasma membrane aquaporins (Törnroth-Horsefield et al., 2006).”