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Cytoplasm localization of aminopeptidase M1 and its functional activity in root hair cells and BY-2 cells

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Abstract

Aminopeptidase M1 (APM1) was the first M1 metallopeptidase family member identified in Arabidopsis, isolated by its affinity for the auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). A loss-of-function mutation showed various developmental defects in cell division and auxin transport. APM1 was shown to be localized in endomembrane structures, the cytoplasm, and the plasma membrane. These previous results suggested that APM1 has diverse functional roles in different cell and tissue types. Here we report that APM1 localized to the cytoplasm, and its over-expression in the root hair cell caused longer root hair phenotypes. Treatment of aminopeptidase inhibitors caused internalization of auxin efflux PIN-FORMED proteins in root hair cells and suppressed short root hair phenotype of PIN3 overexpression line (PIN3ox). APM1 also localized to the cytoplasm in tobacco BY-2 cells, its over-expression had little effect on auxin transport in these cells.

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Abbreviations

1-NAA:

Naphthalene-1-acetic acid

IAA:

Indole-3-acetic acid

DEX:

Dexamethasone

YFP:

Yellow fluorescence protein

BY-2:

Bright Yellow-2

NPA:

N-1-naphthylphthalamic acid

PAT:

Polar auxin transport

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Acknowledgments

We thank Jiřĭ Friml at Ghent University for providing P PIN2 :PIN2-GFP seeds and Yuichi Hashimoto at University of Tokyo for providing PAQ22. This research was supported by grants from the Mid-career Researcher Program (2011-0017242, NRF, MEST), the Next-Generation BioGreen 21 programs (TAGC PJ00820701 and SSAC PJ00814102) of the Rural Development Administration to HTC, and the Basic Research Program through the National Research Foundation of Korea (NRF) funded by the ministry of Education, Science and Technology (2011-0008135) to ORL.

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Correspondence to Hyung-Taeg Cho.

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Lee, O.R., Cho, HT. Cytoplasm localization of aminopeptidase M1 and its functional activity in root hair cells and BY-2 cells. Mol Biol Rep 39, 10211–10218 (2012). https://doi.org/10.1007/s11033-012-1896-1

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