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NIP1;1, an aquaporin homolog, determines the arsenite sensitivity of Arabidopsis thaliana.

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Arsenite [As(III)] is highly toxic to organisms, including plants. Very recently, transporters in rice responsible for As(III) transport have been described (Ma, J. F., Yamaji, N., Mitani, N., Xu, X. Y., Su, Y. H., McGrath, S. P., and Zhao, F. J. (2008) Proc. Natl. Acad. Sci. U. S. A. 105,

Genome-wide Association Study Reveals that the Aquaporin NIP1;1 Contributes to Variation in Hydrogen Peroxide Sensitivity in Arabidopsis thaliana.

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Hydrogen peroxide (H2O2) is a reactive oxygen species that affects cell signaling in various plant defense responses and induces programmed cell death. To identify the new components associated with H2O2 signaling and tolerance, we conducted a genome-wide association study (GWAS) on the root growth

Arabidopsis thaliana NIP7;1: an anther-specific boric acid transporter of the aquaporin superfamily regulated by an unusual tyrosine in helix 2 of the transport pore.

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Plant nodulin-26 intrinsic proteins (NIPs) are members of the aquaporin superfamily that serve as multifunctional transporters of uncharged metabolites. In Arabidopsis thaliana, a specific NIP pore subclass, known as the NIP II proteins, is represented by AtNIP5;1 and AtNIP6;1, which encode channel

A defect in the yeast plasma membrane urea transporter Dur3p is complemented by CpNIP1, a Nod26-like protein from zucchini (Cucurbita pepo L.), and by Arabidopsis thaliana delta-TIP or gamma-TIP.

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Dur3 encodes the yeast plasma membrane urea transporter and Deltadur3 mutants are unable to grow on media containing low concentrations of urea as sole nitrogen source. Complementation of the Deltadur3 mutant line with expression libraries generated from whole Arabidopsis thaliana seedlings or from

Aquaporin NIP2;1 is mainly localized to the ER membrane and shows root-specific accumulation in Arabidopsis thaliana.

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We investigated a nodulin 26-like protein NIP2;1, which belongs to the third subgroup of Arabidopsis aquaporins. Histochemical analysis of a promoter-beta-glucuronidase fusion revealed the root-specific expression of NIP2;1. The NIP2;1 protein was detected in young roots, but not in leaves, stems,

Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana.

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Although arsenite [As(III)] is non-essential and toxic for plants, it is effectively absorbed through various transporters into the roots. Here we identified a calcium-dependent protein kinase (CPK31) response for As(III) tolerance in Arabidopsis. We identified CPK31 as an interacting protein of a

Arabidopsis NIP1;1 transports antimonite and determines antimonite sensitivity.

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Antimony (Sb) is toxic to organisms including plants. Although it is not essential to organisms, plants take up Sb from the environment. In this study, we identified an antimonite [Sb(III)] transporter from Arabidopsis thaliana. We examined the Sb(III) tolerance of the disruption mutant plants of

Expanding roles of plant aquaporins in plasma membranes and cell organelles

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Aquaporins facilitate water transport across biomembranes in a manner dependent on osmotic pressure and water-potential gradient. The discovery of aquaporins has facilitated research on intracellular and whole-plant water transport at the molecular level. Aquaporins belong to a ubiquitous family of

ER membrane aquaporins in plants.

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Plant has a large aquaporin family with more than 30 members which are divided into four subfamilies: plasma membrane intrinsic protein (PIP), tonoplast intrinsic protein (TIP), nodulin 26-like intrinsic proteins (NIP), and small and basic intrinsic proteins (SIP). Their primary structure, transport

Arabidopsis NIP2;1, a major intrinsic protein transporter of lactic acid induced by anoxic stress.

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Nodulin 26 intrinsic proteins (NIPs) are plant-specific, highly conserved water and solute transport proteins with structural and functional homology to soybean nodulin 26. Arabidopsis thaliana contains nine NIP genes. In this study, it is shown that one of these, AtNIP2;1, is exquisitely sensitive

Polar Localization of the NIP5;1 Boric Acid Channel Is Maintained by Endocytosis and Facilitates Boron Transport in Arabidopsis Roots.

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Boron uptake in Arabidopsis thaliana is mediated by nodulin 26-like intrinsic protein 5;1 (NIP5;1), a boric acid channel that is located preferentially on the soil side of the plasma membrane in root cells. However, the mechanism underlying this polar localization is poorly understood. Here, we show

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