These authors contributed equally to this work.
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Original Article
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Identification and functional characterization of the Arabidopsis Snf1-related protein kinase SnRK2.4 phosphatidic acid-binding domain
Article first published online: 1 SEP 2014
DOI: 10.1111/pce.12421
© 2014 The Authors. Plant, Cell & Environment published by John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
Additional Information
How to Cite
JULKOWSKA, M. M., MCLOUGHLIN, F., GALVAN-AMPUDIA, C. S., RANKENBERG, J. M., KAWA, D., KLIMECKA, M., HARING, M. A., MUNNIK, T., KOOIJMAN, E. E. and TESTERINK, C. (2015), Identification and functional characterization of the Arabidopsis Snf1-related protein kinase SnRK2.4 phosphatidic acid-binding domain. Plant, Cell & Environment, 38: 614–624. doi: 10.1111/pce.12421
Publication History
- Issue published online: 14 FEB 2015
- Article first published online: 1 SEP 2014
- Accepted manuscript online: 30 JUL 2014 05:30AM EST
- Manuscript Accepted: 20 JUL 2014
- Manuscript Revised: 17 JUL 2014
- Manuscript Received: 15 APR 2014
Funded by
- Netherlands Organisation for Scientific Research (NWO). Grant Numbers: Vidi 700.56.429, ALW 820.02.017, ALW 846.11.002
- STW Learning from Nature. Grant Number: 10987
- NGI Horizon. Grant Number: 93511011
- U.S. National Science Foundation I2CAM International Materials Institute Award. Grant Number: DMR-0844115
Keywords:
- phosphatidic acid;
- phospholipid binding;
- root system architecture;
- SnRK2.10
Abstract
Phosphatidic acid (PA) is an important signalling lipid involved in various stress-induced signalling cascades. Two SnRK2 protein kinases (SnRK2.4 and SnRK2.10), previously identified as PA-binding proteins, are shown here to prefer binding to PA over other anionic phospholipids and to associate with cellular membranes in response to salt stress in Arabidopsis roots. A 42 amino acid sequence was identified as the primary PA-binding domain (PABD) of SnRK2.4. Unlike the full-length SnRK2.4, neither the PABD-YFP fusion protein nor the SnRK2.10 re-localized into punctate structures upon salt stress treatment, showing that additional domains of the SnRK2.4 protein are required for its re-localization during salt stress. Within the PABD, five basic amino acids, conserved in class 1 SnRK2s, were found to be necessary for PA binding. Remarkably, plants overexpressing the PABD, but not a non-PA-binding mutant version, showed a severe reduction in root growth. Together, this study biochemically characterizes the PA–SnRK2.4 interaction and shows that functionality of the SnRK2.4 PABD affects root development.
