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Plant and Cell Physiology Advance Access originally published online on September 5, 2006
Plant and Cell Physiology 2006 47(10):1420-1426; doi:10.1093/pcp/pcl004
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© The Author 2006. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Short Communication

Aquaporin NIP2;1 is Mainly Localized to the ER Membrane and Shows Root-Specific Accumulation in Arabidopsis thaliana

Masahiro Mizutani1, Satoshi Watanabe1, Tsuyoshi Nakagawa2 and Masayoshi Maeshima1,*

1Laboratory of Cell Dynamics, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601 Japan
2Department of Molecular and Functional Genomics, Shimane University, Matsue, 690-8504 Japan

* Corresponding author: E-mail, maeshima{at}agr.nagoya-u.ac.jp; Fax, +81-52-789-4096.

We investigated a nodulin 26-like protein NIP2;1, which belongs to the third subgroup of Arabidopsis aquaporins. Histochemical analysis of a promoter–ß-glucuronidase fusion revealed the root-specific expression of NIP2;1. The NIP2;1 protein was detected in young roots, but not in leaves, stems, flowers or siliques. The transient expression of NIP2;1 linked with green fluorescent protein in Arabidopsis cultured cells showed its putative endoplasmic reticulum (ER) localization. NIP2;1 expressed in yeast cells had low water channel activity in the membranes. NIP2;1 may function as a water channel and/or ER channel for other small molecules or ions.

(Received July 5, 2006; Accepted August 28, 2006)
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