A receptor-like protein acts as a specificity switch for the regulation of stomatal development
- Guangzhong Lin1,2,
- Liang Zhang3,
- Zhifu Han1,
- Xinru Yang1,
- Weijia Liu1,
- Ertong Li4,
- Junbiao Chang5,
- Yijun Qi6,
- Elena D. Shpak3 and
- Jijie Chai1,6,7,8
- 1Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China;
- 2College of Life Sciences, Peking University, Beijing 100871, China;
- 3Biochemistry, Cellular, and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996, USA;
- 4College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou 450001, China;
- 5Collaborative Innovation Center of New Drug Research and Safety Evaluation, Zhengzhou University, Zhengzhou 450001, China;
- 6Center for Plant Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;
- 7Max-Planck Institute for Plant Breeding Research, 50829 Cologne, Germany;
- 8Institute of Biochemistry, University of Cologne, 50674 Koeln, Germany
- Corresponding author: chaijj{at}tsinghua.edu.cn
Abstract
Stomata are microscopic openings that allow for the exchange of gases between plants and the environment. In Arabidopsis, stomatal patterning is specified by the ERECTA family (ERf) receptor kinases (RKs), the receptor-like protein (RLP) TOO MANY MOUTHS (TMM), and EPIDERMAL PATTERNING FACTOR (EPF) peptides. Here we show that TMM and ER or ER-LIKE1 (ERL1) form constitutive complexes, which recognize EPF1 and EPF2, but the single ERfs do not. TMM interaction with ERL1 creates a binding pocket for recognition of EPF1 and EPF2, indicating that the constitutive TMM–ERf complexes function as the receptors of EPF1 and EPF2. EPFL9 competes with EPF1 and EPF2 for binding to the ERf–TMM complex. EPFL4 and EPFL6, however, are recognized by the single ERfs without the requirement of TMM. In contrast to EPF1,2, the interaction of EPFL4,6 with an ERf is greatly reduced in the presence of TMM. Taken together, our data demonstrate that TMM dictates the specificity of ERfs for the perception of different EPFs, thus functioning as a specificity switch for the regulation of the activities of ERfs.
Keywords
- biochemical interaction
- peptide hormones
- receptor kinases
- receptor-like protein
- stomatal development
- structure
Footnotes
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Supplemental material is available for this article.
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Article published online ahead of print. Article and publication date are online at http://www.genesdev.org/cgi/doi/10.1101/gad.297580.117.
- Received February 15, 2017.
- Accepted April 28, 2017.
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