With respect to their animal counte

With respect to their animal counterparts, plant aquaporins show a
broader array of sub-cellular localizations, in relation with the high
degree of compartmentalization of plant cells. Aquaporins have been
localized in nearly all of plant cell sub-cellular compartments, including
plasma membrane, tonoplast, ER, Golgi apparatus and chloroplast.
Localization of aquaporins in the chloroplast, which quasi exclusively
relies on proteomic studies, is still debated [16]. Interestingly, some
aquaporins exhibit multiple sub-cellular localizations. For instance,
NtAQP1, a tobacco PIP1 homolog, was observed in both the plasma
membrane and chloroplast inner envelope membrane of tobacco leaf
cells [17]. Seed-specific TIPs of Arabidopsis (AtTIP3;1, AtTIP3;2), which
predominantly sit in the protein storage vacuoles, are also transiently
expressed at the plasma membrane during the early stages of seed
germination and maturation [18]. In these two cases, however, it will
be important that these observations can be extended to other plant
species. Several mechanisms that determine the trafficking of newly
synthesized PIPs or TIPs to their destination membranes have recently
been discovered. In PIP2s, diacidic motifs and C-terminal phosphorylation
were found to favor export from the ER [19–21]. In contrast,
homologs of the PIP1 sub-class showed trafficking defects, unless they
were co-expressed with PIP2s and formed heterotetramers [21–23].
These molecular interactions seem to be necessary for PIP1s to reach
the plasma membrane (see 4.3). In addition, a role for Soluble NSF
Attachment Protein REceptors (SNAREs) in PIP trafficking to the plasma
membrane was recently uncovered [24,25]. However, the mechanisms
that determine the multiple localizations of some aquaporins are as
yet unknown

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