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Plant and Cell Physiology Advance Access published online on September 5, 2006
Plant and Cell Physiology, 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 e-mail: 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 Mizutani 1, Satoshi Watanabe 1, Tsuyoshi Nakagawa 2, and Masayoshi Maeshima 1 *

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

* To whom correspondence should be addressed.
Masayoshi Maeshima, E-mail: maeshima{at}agr.nagoya-u.ac.jp


  Abstract

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, flowers or siliques. The transient expression of NIP2;1 linked with green fluorescent protein in Arabidopsis cultured cells showed its putative 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.

Keywords: Aquaporin; Arabidopsis; ER; NIP; Root; Water channel.
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