Pollen Aquaporins: The Solute Factor

Giorgio, Juliana Andrea Pérez Di; Soto, Gabriela; Muschietti, Jorge; Amodeo, Gabriela

doi:10.3389/fpls.2016.01659

Cited by 10 publications

(6 citation statements)

References 80 publications

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“…No interaction between SYP131 and PIP2;7 was reported in SUS assays by Jones et al (2014) and no PIP2;7 expression was reported in the pollen in proPIP2;7:GUS lines ( Da Ines, 2008 ; Prado et al, 2013 ; Hachez et al, 2014 ). However, large-scale data revealed that PIP2;7/2;8 (the probe used cannot differentiate between both isoforms), are expressed during pollen development but not in mature pollen ( Pérez Di Giorgio et al, 2016 ).…”

Section: Discussionmentioning

confidence: 99%

Interaction Between the SNARE SYP121 and the Plasma Membrane Aquaporin PIP2;7 Involves Different Protein Domains

et al. 2021

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Plasma membrane intrinsic proteins (PIPs) are channels facilitating the passive diffusion of water and small solutes. Arabidopsis PIP2;7 trafficking occurs through physical interaction with SNARE proteins including the syntaxin SYP121, a plasma membrane Qa-SNARE involved in membrane fusion. To better understand the interaction mechanism, we aimed at identifying the interaction motifs in SYP121 and PIP2;7 using ratiometric bimolecular fluorescence complementation assays in Nicotiana benthamiana. SYP121 consists of four regions, N, H, Q, and C, and sequential deletions revealed that the C region, containing the transmembrane domain, as well as the H and Q regions, containing the Habc and Qa-SNARE functional domains, interact with PIP2;7. Neither the linker between the Habc and the Qa-SNARE domains nor the H or Q regions alone could fully restore the interaction with PIP2;7, suggesting that the interacting motif depends on the conformation taken by the HQ region. When investigating the interacting motif(s) in PIP2;7, we observed that deletion of the cytosolic N- and/or C- terminus led to a significant decrease in the interaction with SYP121. Shorter deletions revealed that at the N-terminal amino acid residues 18–26 were involved in the interaction. Domain swapping experiments between PIP2;7 and PIP2;6, a PIP isoform that does not interact with SYP121, showed that PIP2;7 N-terminal part up to the loop C was required to restore the full interaction signal, suggesting that, as it is the case for SYP121, the interaction motif(s) in PIP2;7 depend on the protein conformation. Finally, we also showed that PIP2;7 physically interacted with other Arabidopsis SYP1s and SYP121 orthologs.

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Section: Discussionmentioning

confidence: 99%

Interaction Between the SNARE SYP121 and the Plasma Membrane Aquaporin PIP2;7 Involves Different Protein Domains

et al. 2021

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“…In tobacco, PIP genes are suggested to be involved in the movement of water between pollen and stigma ( Bots et al, 2005 ). However, the role of TIP1-1 and TIP2-1 in pistil remains elusive ( Pérez Di Giorgio et al, 2016 ).…”

Section: Resultsmentioning

confidence: 99%

RNA-Seq Highlights Molecular Events Associated With Impaired Pollen-Pistil Interactions Following Short-Term Heat Stress in Brassica napus

2021

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The global climate change is leading to increased frequency of heatwaves with crops getting exposed to extreme temperature events. Such temperature spikes during the reproductive stage of plant development can harm crop fertility and productivity. Here we report the response of short-term heat stress events on the pollen and pistil tissues in a commercially grown cultivar of Brassica napus. Our data reveals that short-term temperature spikes not only affect pollen fitness but also impair the ability of the pistil to support pollen germination and pollen tube growth and that the heat stress sensitivity of pistil can have severe consequences for seed set and yield. Comparative transcriptome profiling of non-stressed and heat-stressed (40°C for 30 min) pollen and pistil (stigma + style) highlighted the underlying cellular mechanisms involved in heat stress response in these reproductive tissues. In pollen, cell wall organization and cellular transport-related genes possibly regulate pollen fitness under heat stress while the heat stress-induced repression of transcription factor encoding transcripts is a feature of the pistil response. Overall, high temperature altered the expression of genes involved in protein processing, regulation of transcription, pollen-pistil interactions, and misregulation of cellular organization, transport, and metabolism. Our results show that short episodes of high-temperature exposure in B. napus modulate key regulatory pathways disrupted reproductive processes, ultimately translating to yield loss. Further investigations on the genes and networks identified in the present study pave a way toward genetic improvement of the thermotolerance and reproductive performance of B. napus varieties.

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“…Besides studies in plants and animals that have been separately presented, there are features that can be compared, such as those described in the reproductive systems. In plants, specific pollen AQPs have been reported, such as TIP1;3, TIP5;1, NIP4;1 and NIP4;2 (Soto et al 2008;Pérez Di Giorgio et al 2016a, 2016b. These reproduction-associated AQPs showed low water permeability but the capacity to transport glycerol and urea, and have been suggested to be involved in the nitrogen metabolic pathway during pollen tube growth (Soto et al 2008(Soto et al , 2010Pérez Di Giorgio et al 2016a, b).…”

Section: The Pathological Focus In Animalsmentioning

confidence: 99%

“…Since the first water channel report (Preston et al 1992), the discovery of AQPs had a significant impact on the study of water and solute transport. However, the view of AQPs as specific water channels has been changing due to large amount of evidence showing that some AQPs carry small solutes or gases, and others are expressed in tissues where water flow dynamics appear to be less relevant (Bienert et al 2008;Kitchen et al 2015b;Pérez Di Giorgio et al 2016a, 2016b.…”

Section: What Are Aqps Formentioning

confidence: 99%

“…The following experimental evidence suggested that AQPs could be an osmosensor located in the plasma membrane of growing pollen tubes of Lilium longiflorum (Shachar- Hill et al 2013). In Arabidosis thaliana, the most expressed AQPs in pollen are non-orthodox and seem not to be involved in water transport (Pérez Di Giorgio et al 2016a, 2016b. So far, their role is more complex and needs to be elucidated.…”

Section: What Are Aqps Formentioning

confidence: 99%

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Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives

2017

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Aquaporins (AQPs) can be revisited from a distinct and complementary perspective: the outcome from analyzing them from both plant and animal studies. (1) The approach in the study. Diversity found in both kingdoms contrasts with the limited number of crystal structures determined within each group. While the structure of almost half of mammal AQPs was resolved, only a few were resolved in plants. Strikingly, the animal structures resolved are mainly derived from the AQP2-lineage, due to their important roles in water homeostasis regulation in humans. The difference could be attributed to the approach: relevance in animal research is emphasized on pathology and in consequence drug screening that can lead to potential inhibitors, enhancers and/or regulators. By contrast, studies on plants have been mainly focused on the physiological role that AQPs play in growth, development and stress tolerance. (2) The transport capacity. Besides the well-described AQPs with high water transport capacity, large amount of evidence confirms that certain plant AQPs can carry a large list of small solutes. So far, animal AQP list is more restricted. In both kingdoms, there is a great amount of evidence on gas transport, although there is still an unsolved controversy around gas translocation as well as the role of the central pore of the tetramer. (3) More roles than expected. We found it remarkable that the view of AQPs as specific channels has evolved first toward simple transporters to molecules that can experience conformational changes triggered by biochemical and/or mechanical signals, turning them also into signaling components and/or behave as osmosensor molecules.

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Pollen Aquaporins: The Solute Factor

Cited by 10 publications

References 80 publications

Interaction Between the SNARE SYP121 and the Plasma Membrane Aquaporin PIP2;7 Involves Different Protein Domains

Interaction Between the SNARE SYP121 and the Plasma Membrane Aquaporin PIP2;7 Involves Different Protein Domains

RNA-Seq Highlights Molecular Events Associated With Impaired Pollen-Pistil Interactions Following Short-Term Heat Stress in Brassica napus

Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives

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