Functional selectivity for glycerol of the nodulin 26 subfamily of plant membrane intrinsic proteins

Wallace, Ian S.; Wills, David M.; Guenther, James F.; Roberts, Daniel M.

doi:10.1016/s0014-5793(02)02955-1

Cited by 58 publications

(38 citation statements)

References 16 publications

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“…Since all characterized members of the NIP family are aquaglyceroporins (Rivers et al, 1997;Dean et al, 1999;Guenther and Roberts, 2000;Weig and Jakob, 2000), it is argued that the H2 position may be a critical determinant of selectivity. This is supported by the observation that the substitution of the conserved Trp at H2 with a TIP-like His results in the conversion of NIPs to water-selective aquaporins (Wallace et al, 2002).…”

Section: Tip and Nip Subgroupsmentioning

confidence: 77%

“…Nodulin 26 is an aquaglyceroporin with low intrinsic water conductance (Rivers et al, 1997;Dean et al, 1999;Wallace et al, 2002) that is positively regulated by phosphorylation on Ser-262 (Guenther et al, 2003). The nodulin 26 pore is also permeated by some uncharged solutes, such as glycerol, whereas other test solutes (urea and acetamide) are excluded (Rivers et al, 1997).…”

Section: Homology Modeling Plant Mips: Nodulin 26 As a Test Casementioning

confidence: 99%

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Homology Modeling of Representative Subfamilies of Arabidopsis Major Intrinsic Proteins. Classification Based on the Aromatic/Arginine Selectivity Filter

2004

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Major intrinsic proteins (MIPs) are a family of membrane channels that facilitate the bidirectional transport of water and small uncharged solutes such as glycerol. The 35 full-length members of the MIP family in Arabidopsis are segregated into four structurally homologous subfamilies: plasma membrane intrinsic proteins (PIPs), tonoplast intrinsic proteins (TIPs), nodulin 26-like intrinsic membrane proteins (NIPs), and small basic intrinsic proteins (SIPs). Computational methods were used to construct structural models of the putative pore regions of various plant MIPs based on homology modeling with the atomic resolution crystal structures of mammalian aquaporin 1 and the bacterial glycerol permease GlpF. Based on comparisons of the narrow selectivity filter regions (the aromatic/Arg [ar/R] filter), the members of the four phylogenetic subfamilies of Arabidopsis MIPs can be classified into eight groups. PIPs possess a uniform ar/R signature characteristic of high water transport aquaporins, whereas TIPs are highly diverse with three separate conserved ar/R regions. NIPs possess two separate conserved ar/R regions, one that is similar to the archetype, soybean (Glycine max) nodulin 26, and another that is characteristic of Arabidopsis NIP6;1. The SIP subfamily possesses two ar/R subgroups, characteristic of either SIP1 or SIP2. Both SIP ar/R residues are divergent from all other MIPs in plants and other kingdoms. Overall, these findings suggest that higher plant MIPs have a common fold but show distinct differences in proposed pore apertures, potential to form hydrogen bonds with transported molecules, and amphiphilicity that likely results in divergent transport selectivities.Members of the major intrinsic protein (MIP) family form a large and diverse group of membrane proteins that facilitate the bidirectional transport of water and some small solutes across cellular membranes (Agre et al., 2002;Thomas et al., 2002). MIPs are widely distributed in organisms from bacteria to higher eukaryotes, and these proteins are especially abundant in plants, with 35 full-length genes present in Arabidopsis (Johanson et al., 2001;Quigley et al., 2001). Members of the plant MIP family have been implicated in cell elongation and development, changes in hydraulic conductivity in response to environmental cues, and numerous other processes that require rapid transmembrane movements of water (for review, see Johansson et al., 2000;Maurel et al., 2002;Tyerman et al., 2002).MIP family members in Arabidopsis are subdivided into four subfamilies: the plasma membrane intrinsic proteins (PIPs; 13 genes), the tonoplast intrinsic membrane proteins (TIPs; 10 genes), the nodulin 26-like intrinsic membrane proteins (NIPs; 9 genes), and the small basic intrinsic proteins (SIPs; 3 genes) (Weig et al., 1997;Johanson et al., 2001;Quigley et al., 2001). By contrast, mammals have only two functional subfamilies of MIPs: water-specific aquaporins and solute-transporting glyceroporins and aquaglyceroporins (Agre et al., 2002). This disparity leads...

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Section: Tip and Nip Subgroupsmentioning

confidence: 77%

Section: Homology Modeling Plant Mips: Nodulin 26 As a Test Casementioning

confidence: 99%

Homology Modeling of Representative Subfamilies of Arabidopsis Major Intrinsic Proteins. Classification Based on the Aromatic/Arginine Selectivity Filter

2004

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“…Nodulin 26 (Rivers et al, 1997;Dean et al, 1999) and other NIP proteins (Weig et al, 1997;Guenther and Roberts, 2000;Weig and Jakob, 2000) share the general properties of multifunctional transport of water and uncharged solutes such as glycerol and have a low rate of water transport compared with most water-selective aquaporins (Rivers et al, 1997;Dean et al, 1999). Homology modeling based on MIP crystal structures (Fu et al, 2000;Sui et al, 2001) reveal a unique "hybrid" signature of four amino acids within the selectivity filter of the NIP pore that are proposed to account for these transport properties (Wallace et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of Soybean Nodulin 26 on Serine 262 Enhances Water Permeability and Is Regulated Developmentally and by Osmotic Signals

et al. 2003

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Soybean nodulin 26 is expressed and targeted to the symbiosome membrane of nitrogen-fixing nodules, where it forms an aquaporin channel with a modest water transport rate. In this study, we show that the phosphorylation of nodulin 26 on Ser-262, which is catalyzed by a symbiosome membrane-associated calcium-dependent protein kinase, stimulates its intrinsic water transport rate. Furthermore, using a phosphospecific antibody, we have elucidated the developmental appearance and regulation of nodulin 26 phosphorylation in vivo. Although nodulin 26 protein is detected first in differentiating infected cells (16 days), phosphorylated nodulin 26 does not become pronounced until infected cell maturation (25 days). Phosphorylation is sustained at steady state levels until entry into senescence. Nodulin 26 phosphorylation is enhanced further by osmotic stresses (water deprivation and salinity). Thus, the phosphorylation of nodulin 26 coincides with the establishment of mature nitrogen-fixing symbiosomes, is regulated by osmotic stresses that induce calcium-signaling pathways, and appears to be part of the adaptive responses of infected cells to osmotic challenge.

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“…The tryptophan side-chain is also present in PsNIP-1 and all other members of the NIP subfamily that have been experimentally characterized as aquaglyceroporins (Table 1). The importance of the tryptophan residue for glycerol permeation was recently demonstrated for LIMP2 (Wallace et al, 2002). Some NIPs, however, do not contain this tryptophan residue (not shown), and their permeation characteristics have yet to be determined.…”

Section: An Aquaglyceroporin Is Specifically Expressed In the Seed Coatmentioning

confidence: 95%

Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies

et al. 2003

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Water and nutrients required by developing seeds are mainly supplied by the phloem and have to be released from a maternal parenchyma tissue before being utilized by the filial tissues of embryo and endosperm. To identify aquaporins that could be involved in this process four full-length cDNAs were cloned and sequenced from a cDNA library of developing seed coats of pea (Pisum sativum L.). The cDNA of PsPIP1-1 appeared to be identical to that of clone 7a/TRG-31, a turgor-responsive gene cloned previously from pea roots. PsPIP1-1, PsPIP2-1, and PsTIP1-1, or their possible close homologues, were also expressed in cotyledons of developing and germinating seeds, and in roots and shoots of seedlings, but transcripts of PsNIP-1 were only detected in the seed coat. In mature dry seeds, high hybridization signals were observed with the probe for PsPIP1-1, but transcripts of PsPIP2-1, PsTIP1-1, and PsNIP-1 were not detected. Functional characterization after heterologous expression in Xenopus oocytes showed that PsPIP2-1 and PsTIP1-1 are aquaporins whereas PsNIP-1 is an aquaglyceroporin. PsNIP-1, like several other NIPs, contains a tryptophan residue corresponding with Trp-48 in GlpF (the glycerol facilitator of Escherichia coli) that borders the selectivity filter in the permeation channel. It is suggested that PsPIP1-1 and/or its possible close homologues could play a role in water absorption during seed imbibition, and that PsPIP2-1, possibly together with PsPIP1-1, could be involved in the release of phloem water from the seed coat symplast, which is intimately connected with the release of nutrients for the embryo.Abbreviations: MIPs, major intrinsic proteins; NIPs, nodulin 26-like intrinsic proteins; PIPs, plasma membrane intrinsic proteins; SIPs, small, basic intrinsic proteins; TIPs, tonoplast intrinsic proteins

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Functional selectivity for glycerol of the nodulin 26 subfamily of plant membrane intrinsic proteins

Cited by 58 publications

References 16 publications

Homology Modeling of Representative Subfamilies of Arabidopsis Major Intrinsic Proteins. Classification Based on the Aromatic/Arginine Selectivity Filter

Homology Modeling of Representative Subfamilies of Arabidopsis Major Intrinsic Proteins. Classification Based on the Aromatic/Arginine Selectivity Filter

Phosphorylation of Soybean Nodulin 26 on Serine 262 Enhances Water Permeability and Is Regulated Developmentally and by Osmotic Signals

Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies

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