Plasma Membrane Aquaporins in the Motor Cells of <i>Samanea saman</i>

Moshelion, Menachem; Becker, Dirk; Biela, Alexander; Uehlein, Norbert; Hedrich, Rainer; Otto, Beate; Levi, Hadas; Moran, Nava; Kaldenhoff, Ralf

doi:10.1105/tpc.010351

Cited by 200 publications

(139 citation statements)

References 40 publications

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“…MIPs have a broad range of transport selectivity with various members permeable to water (Biela et al 1999;Santoni et al 2000;Tyerman et al 2002), glycerol (Biela et al 1999;Weig and Jakob 2000;Moshelion et al 2002), urea (Gerbeau et al 1999), CO 2 (Uehlein et al 2003), NH 3 (Jahn et al 2004;Loque et al 2005), silicon (Ma et al 2006) boron (Takano et al 2006;Tanaka et al 2008) and arsenite (Kamiya et al 2009). The PIP2 members have been shown to have high water permeability, though there are exceptions (Zhou et al 2007), and PIP1s have low water permeability or no apparent permeability.…”

Section: Introductionmentioning

confidence: 99%

Identification and functional characterisation of aquaporins in the grapevine, Vitis vinifera

Shelden

Howitt

Kaiser

et al. 2009

Functional Plant Biol.

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Abstract. Plant aquaporins belong to a large superfamily of conserved proteins called the major intrinsic proteins (MIPs).There is limited information about the diversity of MIPs in grapevine, and their water transport capacity. The aim of the present study was to identify MIPs from grapevine and functionally characterise water transport of a subset of MIPs. Candidate genes were identified, by screening a Vitis vinifera L. (cv. Cabernet Sauvignon) cDNA library with gene specific probes, for aquaporin cDNAs encoding members of the plasma membrane intrinsic protein (PIP) and tonoplast intrinsic protein (TIP) subfamilies. The screen resulted in the identification of 11 full-length and two partial length aquaporin cDNAs. VvTIP2;1 isoforms had different 3 0 UTRs, immediately upstream of the poly(A) tail, suggesting the presence of multiple cleavage sites for polyadenylation. Using published genome sequences of grapevine, we conducted a phylogenetic analysis of the MIPs with previously characterised MIPs from Arabidopsis. We identified 23 full-length MIP genes from the V. vinifera genome sequence of a near homozygous line (PN40024) that cluster into the four main subfamilies (and subgroups within) identified in other species. However, based on the identification of PIP2 genes in Cabernet Sauvignon that were not present in the PN40024 genome, there are likely to be more than 23 MIP genes in other heterozygous grapevine cultivars. Water transport capacity was determined for several PIPs and TIPs, by expression in Xenopus oocytes. Only VvPIP2 and VvTIP proteins function as water channels with the exception of VvPIP2;5. VvPIP2;5 differs from the water conducting VvPIP2;1 by the substitution of two highly conserved amino acids in Loop B (G97S, G100W), which was shown by homology modelling to likely form a hydrophobic block of the water pore.

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Section: Introductionmentioning

confidence: 99%

Identification and functional characterisation of aquaporins in the grapevine, Vitis vinifera

Shelden

Howitt

Kaiser

et al. 2009

Functional Plant Biol.

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“…Compared with PIP1 proteins, PIP2 proteins have a shorter N-terminal extension and a longer C terminus (11)(12)(13)(14). In general, plant PIP2 proteins have been shown to facilitate membrane water transport in heterologous expression systems; however, PIP1 proteins display low or no activity in this respect (8,11,(15)(16)(17)(18). For the human AQP1 as well as for the tobacco PIP1 aquaporin NtAQP1, an increased cellular acidification rate under CO 2 -enriched buffer was obtained in oocytes expressing the respective aquaporin in addition to a carbonic anhydrase (9,19,20).…”

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confidence: 99%

Aquaporin Tetramer Composition Modifies the Function of Tobacco Aquaporins

Otto

Uehlein

Sdorra

et al. 2010

Journal of Biological Chemistry

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Heterologous expression in yeast cells revealed that NtAQP1, a member of the so-called PIP1 aquaporin subfamily, did not display increased water transport activity in comparison with controls. Instead, an increased CO 2 -triggered intracellular acidification was observed. NtPIP2;1, which belongs to the PIP2 subfamily of plant aquaporins, behaved as a true aquaporin but lacked a CO 2 -related function. Results from split YFP experiments, protein chromatography, and gel electrophoresis indicated that the proteins form heterotetramers when coexpressed in yeast. Tetramer composition had effects on transport activity as demonstrated by analysis of artificial heterotetramers with a defined proportion of NtAQP1 to NtPIP2;1. A single NtPIP2;1 aquaporin in a tetramer was sufficient to significantly increase the water permeability of the respective yeast cells. With regard to CO 2 -triggered intracellular acidification, a cooperative effect was observed, where maximum rates were measured when the tetramer consisted of NtAQP1 aquaporins only. The results confirm the model of an aquaporin monomer as a functional unit for water transport and suggest that, for CO 2 -related transport processes, a structure built up by the tetramer is the basis of this function.Water moves across biological membranes by diffusion. In most living organisms, the rate of water diffusion can be increased via pore-forming transmembrane proteins, the socalled aquaporins. These consist of six-membrane-spanning helices; N and C termini of the proteins face the cytosol. The helix-connecting loops B and E are themselves short helices that dip into the membrane from opposite sides and form the water-conducting channel (1, 2). Aquaporin monomers can assemble into tetramers (3, 4). Evidence for their function as water transport facilitators was observed by results from experiments using heterologous expression systems, such as Xenopus laevis oocytes (5). Despite this initially detected function, a facilitated membrane transport for glycerol or volatile substances like CO 2 or NH 3 was postulated (6 -9). Plant aquaporins were subdivided into protein groups according to the cellular location in which they have been initially detected and on the basis of sequence similarities (10). Accordingly, the PIPs (plasma membrane-intrinsic proteins) were split into two major groups, the PIP1 and PIP2 aquaporins. Compared with PIP1 proteins, PIP2 proteins have a shorter N-terminal extension and a longer C terminus (11)(12)(13)(14). In general, plant PIP2 proteins have been shown to facilitate membrane water transport in heterologous expression systems; however, PIP1 proteins display low or no activity in this respect (8,11,(15)(16)(17)(18). For the human AQP1 as well as for the tobacco PIP1 aquaporin NtAQP1, an increased cellular acidification rate under CO 2 -enriched buffer was obtained in oocytes expressing the respective aquaporin in addition to a carbonic anhydrase (9,19,20). The observations on NtAQP1, together with the fact that plants deficient in NtAQP1 express...

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“…The PIP1 class of plant aquaporins has been known to possess extended N-terminus and short C-terminus. The PIP1 clade of plant aquaporins includes member proteins that have low water regulation activity in different expression assays as observed in PIP isoforms of Samanea saman (Moshelion et al, 2002). These proteins are generally involved in the conductivity of solutes across plasma membranes (Fetter et al, 2004).…”

Section: Resultsmentioning

confidence: 99%

“…The members of PIP2 aquaporins have been reported from different plant species. The in vitro Xenopus laevis oocyte expression analysis of PIP2 aquaporins indicated 5-20-fold increased water permeability in response to increased turgor pressure (Weig et al, 1997;Moshelion et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of plasma membrane aquaporins isolated from fiber cells of Calotropis procera

Aslam

Khatoon

Cheema

et al. 2013

J. Zhejiang Univ. Sci. B

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Abstract:Calotropis procera, commonly known as "milkweed", possesses long seed trichomes for seed dispersal and has the ability to survive under harsh conditions such as drought and salinity. Aquaporins are water channel proteins expressed in all land plants, divided into five subfamilies plasma membrane intrinsic proteins (PIPs), tonoplast intrinsic proteins (TIPs), NOD26-like proteins (NIPs), small basic intrinsic proteins (SIPs), and the unfamiliar X intrinsic proteins (XIPs). PIPs constitute the largest group of water channel proteins that are involved in different developmental and regulatory mechanisms including water permeability, cell elongation, and stomata opening. Aquaporins are also involved in abiotic stress tolerance and cell expansion mechanisms, but their role in seed trichomes (fiber cells) has never been investigated. A large number of clones isolated from C. procera fiber cDNA library showed sequence homology to PIPs. Both expressed sequence tags (ESTs) and real-time polymerase chain reaction (PCR) studies revealed that the transcript abundance of this gene family in fiber cells of C. procera is greater than that of cotton. Full-length cDNAs of CpPIP1 and CpPIP2 were isolated from C. procera fiber cDNA library and used for constructing plant expression vectors under constitutive (2×35S) and trichome-specific (GhLTP3) promoters. Transgenic tobacco plants were developed via Agrobacterium-mediated transformation. The phenotypic characteristics of the plants were observed after confirming the integration of transgene in plants. It was observed that CpPIP2 expression cassette under 2×35S and GhLTP3 promoter enhanced the numbers of stem and leave trichomes. However, 2×35S::CpPIP2 has a more amplified effect on trichome density and length than GhLTP3::CpPIP2 and other PIP constructs. These findings imply the role of C. procera PIP aquaporins in fiber cell elongation. The PIPs-derived cell expansion mechanism may be exploited through transgenic approaches for improvement of fiber staple length in cotton and boosting of defense against sucking insects by enhancing plant pubescence.

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Plasma Membrane Aquaporins in the Motor Cells of Samanea saman

Cited by 200 publications

References 40 publications

Identification and functional characterisation of aquaporins in the grapevine, Vitis vinifera

Identification and functional characterisation of aquaporins in the grapevine, Vitis vinifera

Aquaporin Tetramer Composition Modifies the Function of Tobacco Aquaporins

Identification and characterization of plasma membrane aquaporins isolated from fiber cells of Calotropis procera

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