PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development

Bots, Marc; Feron, Richard; Uehlein, Norbert; Weterings, Koen; Kaldenhoff, Ralf; Mariani, Titti

doi:10.1093/jxb/eri009

Cited by 43 publications

(56 citation statements)

References 33 publications

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“…Some authors reported high expression of PIP2 in other tissues such as leaves (Sakurai et al, 2008), stigmas (Bots et al, 2005), and flower petals (Ma et al, 2008). To our knowledge, this is the first report of in situ hybridization of PIP2 in the stem liber of trees.…”

Section: Discussion Ethrel Induced a Concomitant Increase In Latex Yimentioning

confidence: 55%

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Involvement of HbPIP2;1 and HbTIP1;1 Aquaporins in Ethylene Stimulation of Latex Yield through Regulation of Water Exchanges between Inner Liber and Latex Cells in Hevea brasiliensis

et al. 2009

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Natural rubber is synthesized in specialized articulated cells (laticifers) located in the inner liber of Hevea brasiliensis. Upon bark tapping, the laticifer cytoplasm (latex) is expelled due to liber tissue turgor pressure. In mature virgin (untapped) trees, shortterm kinetic studies confirmed that ethylene, the rubber yield stimulant used worldwide, increased latex yield, with a concomitant decrease in latex total solid content, probably through water influx in the laticifers. As the mature laticifers are devoid of plasmodesmata, the rapid water exchanges with surrounding liber cells probably occur via the aquaporin pathway. Two full-length aquaporin cDNAs (HbPIP2;1 and HbTIP1;1, for plasma membrane intrinsic protein and tonoplast intrinsic protein, respectively) were cloned and characterized. The higher efficiency of HbPIP2;1 than HbTIP1;1 in increasing plasmalemma water conductance was verified in Xenopus laevis oocytes. HbPIP2;1 was insensitive to HgCl 2 . In situ hybridization demonstrated that HbPIP2;1 was expressed in all liber tissues in the young stem, including the laticifers. HbPIP2;1 was upregulated in both liber tissues and laticifers, whereas HbTIP1;1 was down-regulated in liber tissues but up-regulated in laticifers in response to bark Ethrel treatment. Ethylene-induced HbPIP2;1 up-regulation was confirmed by western-blot analysis. The promoter sequences of both genes were cloned and found to harbor, among many others, ethylene-responsive and other chemical-responsive (auxin, copper, and sulfur) elements known to increase latex yield. Increase in latex yield in response to ethylene was emphasized to be linked with water circulation between the laticifers and their surrounding tissues as well as with the probable maintenance of liber tissue turgor, which together favor prolongation of latex flow.

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Section: Discussion Ethrel Induced a Concomitant Increase In Latex Yimentioning

confidence: 55%

“…Microsomal fractions, including plasma membranes, were extracted from the inner liber according to Bots et al (2005). As protein concentrations were similar for all samples but at the limit of detection using the Bio-Rad kit (Supplemental Fig.…”

Section: Western-blot Analysismentioning

confidence: 99%

Involvement of HbPIP2;1 and HbTIP1;1 Aquaporins in Ethylene Stimulation of Latex Yield through Regulation of Water Exchanges between Inner Liber and Latex Cells in Hevea brasiliensis

et al. 2009

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“…Immunogold TEM labeling for another plasma membrane-localized protein, the PIP2 aquaporin (Bots et al, 2005), detected PIP2 in the plasma membrane of wild-type and abcg11 mutant cells ( Figures 4A and 4B). However, no labeling above background was detected in the inclusions ( Figure 4C; see Supplemental Figure 3 online).…”

Section: Abcg12 Trafficking To the Plasma Membrane Is Dependent On Abmentioning

confidence: 99%

“…Immunolabeling of high-pressure frozen material was performed as described (McFarlane et al, 2008). Primary antibodies were 1/50 polyclonal anti-GFP (A6455 from Molecular Probes); 1/20 polyclonal anti-calreticulin, generated against calreticulin from castor bean (Ricinus communis cv Hale), a generous gift from Sean Coughlan (Coughlan et al, 1997); and 1/50 polyclonal anti-PIP2, generated against PIP2 from tobacco (Nicotiana tabacum cv Petit Havana SR1), a generous gift from Ralf Kaldenhoff, (Bots et al, 2005). Secondary antibody was 1/100 10 nm gold-conjugated goat-anti-rabbit (Ted Pella).…”

Section: High-pressure Freezing Tem and Immunogold Labelingmentioning

confidence: 99%

Arabidopsis ABCG Transporters, Which Are Required for Export of Diverse Cuticular Lipids, Dimerize in Different Combinations

et al. 2010

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ATP binding cassette (ABC) transporters play diverse roles, including lipid transport, in all kingdoms. ABCG subfamily transporters that are encoded as half-transporters require dimerization to form a functional ABC transporter. Different dimer combinations that may transport diverse substrates have been predicted from mutant phenotypes. In Arabidopsis thaliana, mutant analyses have shown that ABCG11/WBC11 and ABCG12/CER5 are required for lipid export from the epidermis to the protective cuticle. The objective of this study was to determine whether ABCG11 and ABCG12 interact with themselves or each other using bimolecular fluorescence complementation (BiFC) and protein traffic assays in vivo. With BiFC, ABCG11/ABCG12 heterodimers and ABCG11 homodimers were detected, while ABCG12 homodimers were not. Fluorescently tagged ABCG11 or ABCG12 was localized in the stem epidermal cells of abcg11 abcg12 double mutants. ABCG11 could traffic to the plasma membrane in the absence of ABCG12, suggesting that ABCG11 is capable of forming flexible dimer partnerships. By contrast, ABCG12 was retained in the endoplasmic reticulum in the absence of ABCG11, indicating that ABCG12 is only capable of forming a dimer with ABCG11 in epidermal cells. Emerging themes in ABCG transporter biology are that some ABCG proteins are promiscuous, having multiple partnerships, while other ABCG transporters form obligate heterodimers for specialized functions.

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“…The abundance of aquaporins in reproductive organs suggests that these proteins function in plant reproduction. In tobacco, PIP1 and PIP2 show distinct expression patterns during stigma and anther development, and may contribute to the development of these organs in different ways [8,9]. In potato, PIP2a was shown to be highly expressed in the pistil and anther tissues [10].…”

Section: Introductionmentioning

confidence: 99%

Mutation of Aquaporin Gene<em> PIP2;5</em> Postpones Pollen Hydration in Arabidopsis

Ts¹,

Wang²,

N³

et al. 2018

Preprint

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In flowering plants with dry stigmas, pollen hydration involves water movement, which may be facilitated by aquaporins. To explore the possibility underlying this biological process, we identified and characterized a mutant with a T-DNA insertion in PIP2;5, which encodes an aquaporin with water channel activity in the PIP2 subfamily. We monitored the pollination process (pollen hydration, germination, and pollen tube growth) of wild type pollen on stigmas of the mutant and wild type. Pollen hydration was postponed on the stigmas of the mutant, compared with that on wild type stigmas. However, pollen tube germination and growth was unaffected in the mutant. The PIP2;5 protein was located in the cell plasma membrane and was preferentially expressed in the stigma. Based on our results, we concluded that PIP2;5 might play an important role in water movement during pollen hydration.

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PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development

Cited by 43 publications

References 33 publications

Involvement of HbPIP2;1 and HbTIP1;1 Aquaporins in Ethylene Stimulation of Latex Yield through Regulation of Water Exchanges between Inner Liber and Latex Cells in Hevea brasiliensis

Involvement of HbPIP2;1 and HbTIP1;1 Aquaporins in Ethylene Stimulation of Latex Yield through Regulation of Water Exchanges between Inner Liber and Latex Cells in Hevea brasiliensis

Arabidopsis ABCG Transporters, Which Are Required for Export of Diverse Cuticular Lipids, Dimerize in Different Combinations

Mutation of Aquaporin Gene<em> PIP2;5</em> Postpones Pollen Hydration in Arabidopsis

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