Aquaporin OsPIP1;1 promotes rice salt resistance and seed germination

Liu, Chengwei; Fukumoto, Tatsuya; Matsumoto, Tadashi; Gena, Patrizia; Frascaria, Daniele; Kaneko, Tomoyuki; Katsuhara, Maki; Zhong, Shihua; Sun, Xiaofen; Zhu, Yanming; Iwasaki, Isao; Ding, Xiaodong; Calamita, Giuseppe; Kitagawa, Yoshichika

doi:10.1016/j.plaphy.2012.11.018

Cited by 150 publications

(114 citation statements)

References 43 publications

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“…Aquaporins are concentrated in zones of cell division and enlargement, play a major role in governing the movement of water between neighboring cells during seed germination Jain et al 2008). Recent studies have implicated the importance of aquaporins in seed imbibition and subsequent germination (Schuurmans et al 2003; Liu et al 2007; Liu et al 2013;Cardoso et al 2015). The function of seed aquaporins may be related to the water imbibition and activation of the metabolic system in the seed, which results in higher germination (Liu et al 2007 (Beaudette et al 2007), whereas in Populus deltoides roots subjected to copper stress genes encoding plasmalemma (PIP) and tonoplast (TIP) AQPs were downregulated under Cu application (Guerra et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Regulation of Seed Germination and the Role of Aquaporins under Abiotic Stress

Kshetrimayum¹,

Sahoo²,

Panda³

2017

IJEAB

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Section: Introductionmentioning

confidence: 99%

Regulation of Seed Germination and the Role of Aquaporins under Abiotic Stress

Kshetrimayum¹,

Sahoo²,

Panda³

2017

IJEAB

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“…In recent years, studies have indicated the importance of the aquaporins in the imbibition and germination processes of seeds (Schuurmans et al 2003;Liu et al 2007;Liu et al 2013). The greater functionality of the aquaporins in seeds may be related to the water absorption process and activation of the metabolic system of the seed, which leads to higher germination rates (Liu et al 2007).…”

Section: Introductionmentioning

confidence: 99%

“…Among them, one can cite works with rice (Liu et al 2013), tomato (Jain et al 2008), broad bean (Novikova et al 2014), and pea (Veselova & Veselovsky 2006). However, only one data on forest species is currently available (Obroucheva et al 2012).…”

Section: Introductionmentioning

confidence: 99%

Seed imbibition and germination of Plathymenia reticulata Benth. (Fabaceae) affected by mercury: possible role of aquaporins

et al. 2015

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Studies that evaluate the physiological and biochemical mechanisms of germination within forest species are needed in order to improve our understanding of such processes. Mercury and dithiothreitol are indicated as important tools in studies that assess the activity of aquaporins during imbibition and germination of seeds. To investigate the alterations caused by mercury in Plathymenia reticulata seeds, different doses of mercury were used in the presence and absence of dithiothreitol. Mercury had a dose-dependent effect on the seeds; in the most dilute solutions mercury partially inhibited the imbibition process, whereas in the most concentrated solutions it caused the death of the embryos. A delay in the hydration of the seeds may have caused decreased germination as a result of the reduced functionality of the aquaporins that were oxidized by mercury. In the presence of the reducing agent dithiothreitol, the activity of these proteins was restored and the germination process was re-established. These findings indicate the importance of aquaporins in the imbibition and germination stages of P. reticulata seeds, and they provide a better understanding of these important developmental events in plants.

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“…It has been proposed that this process is a consequence of a physical interaction between PIP1 and PIP2, as reported in both homologous (31) and heterologous systems (14, 32). Although there are some PIP1 with the ability to reach the PM on their own (20,27,29), this PIP1-PIP2 interaction seems to be present for several pairs of PIP among different species with functional consequences (14,21,28,(33)(34)(35).…”

mentioning

confidence: 99%

“…In contrast, PIP1 have shown complex heterogeneity in water and solute transport and posttranslational regulation. Many reports show that some PIP1 are nonfunctional in regard to water transport (6,25), whereas other PIP1 act as low-efficiency water channels (26)(27)(28), and a minority group shows activity comparable to that of PIP2 (20,29) or, in contrast, serves as solute channels (25,30).…”

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confidence: 99%

Heteromerization of PIP aquaporins affects their intrinsic permeability

Yaneff

Sigaut

Marquez

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

101

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The plant aquaporin plasma membrane intrinsic proteins (PIP) subfamily represents one of the main gateways for water exchange at the plasma membrane (PM). A fraction of this subfamily, known as PIP1, does not reach the PM unless they are coexpressed with a PIP2 aquaporin. Although ubiquitous and abundantly expressed, the role and properties of PIP1 aquaporins have therefore remained masked. Here, we unravel how FaPIP1;1, a fruit-specific PIP1 aquaporin from Fragaria x ananassa, contributes to the modulation of membrane water permeability (P f ) and pH aquaporin regulation. Our approach was to combine an experimental and mathematical model design to test its activity without affecting its trafficking dynamics. We demonstrate that FaPIP1;1 has a high water channel activity when coexpressed as well as how PIP1-PIP2 affects gating sensitivity in terms of cytosolic acidification. PIP1-PIP2 random heterotetramerization not only allows FaPIP1;1 to arrive at the PM but also produces an enhancement of FaPIP2;1 activity. In this context, we propose that FaPIP1;1 is a key participant in the regulation of water movement across the membranes of cells expressing both aquaporins.T he plasma membrane (PM) is the first barrier that limits water exchange in plant cells. The rate of its water transport capacity is mainly associated with aquaporins. Among the seven aquaporin subfamilies described in the plant kingdom, only plasma membrane intrinsic proteins (PIP) and some members of the nodulin-26-like intrinsic proteins (NIP) and X intrinsic proteins (XIP) subfamilies have been shown to be preferentially localized at the PM (1, 2). Of these, PIP aquaporins appear to have a large role in controlling membrane water permeability, whereas NIP and XIP have been mainly described as solute transporters (2-4). Plant PIP aquaporins represent a conserved subfamily that has been historically divided into two subgroups due to their differences in primary structure, PIP1 and PIP2. Interestingly, PIP aquaporins compose ∼40% of the total aquaporin set, and the PIP1 and PIP2 ratio among different species is relatively constant (5-12). Fig. S1 shows the distribution of all aquaporin genes present in plants whose genome has been completely sequenced and analyzed. Antisense inhibition experiments on Arabidopsis thaliana PIP1 and PIP2 have suggested that the two subgroups of aquaporins contribute to root or leaf hydraulic conductivity in the same way (13). In several plant species, members of the PIP1 and PIP2 subgroups were shown to be coexpressed in the same cell type (14-17).Although PIP1 are as ubiquitous as PIP2, the functional properties of each type of channel are different. PIP2 are very well described as a homotetramer with high water transport activity (18, 19) and a gating mechanism unequivocally associated with specific and conserved amino acid motifs triggered by cytosolic acidification (20-22), phosphorylation (23, 24), or divalent cation concentration (22). In contrast, PIP1 have shown complex heterogeneity in water and solute transpor...

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Aquaporin OsPIP1;1 promotes rice salt resistance and seed germination

Cited by 150 publications

References 43 publications

Regulation of Seed Germination and the Role of Aquaporins under Abiotic Stress

Regulation of Seed Germination and the Role of Aquaporins under Abiotic Stress

Seed imbibition and germination of Plathymenia reticulata Benth. (Fabaceae) affected by mercury: possible role of aquaporins

Heteromerization of PIP aquaporins affects their intrinsic permeability

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