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Science 338 (6105): 390-393

Copyright © 2012 by the American Association for the Advancement of Science

Processing and Subcellular Trafficking of ER-Tethered EIN2 Control Response to Ethylene Gas

Hong Qiao,1 Zhouxin Shen,2 Shao-shan Carol Huang,1,3,4 Robert J. Schmitz,1,3 Mark A. Urich,1,3 Steven P. Briggs,2 Joseph R. Ecker1,3,4,*

Abstract: Ethylene gas is essential for many developmental processes and stress responses in plants. ETHYLENE INSENSITIVE2 (EIN2), an NRAMP-like integral membrane protein, plays an essential role in ethylene signaling, but its function remains enigmatic. Here we report that phosphorylation-regulated proteolytic processing of EIN2 triggers its endoplasmic reticulum (ER)–to–nucleus translocation. ER-tethered EIN2 shows CONSTITUTIVE TRIPLE RESPONSE1 (CTR1) kinase–dependent phosphorylation. Ethylene triggers dephosphorylation at several sites and proteolytic cleavage at one of these sites, resulting in nuclear translocation of a carboxyl-terminal EIN2 fragment (EIN2-C'). Mutations that mimic EIN2 dephosphorylation, or inactivate CTR1, show constitutive cleavage and nuclear localization of EIN2-C' and EIN3 and EIN3-LIKE1–dependent activation of ethylene responses. These findings uncover a mechanism of subcellular communication whereby ethylene stimulates phosphorylation-dependent cleavage and nuclear movement of the EIN2-C' peptide, linking hormone perception and signaling components in the ER with nuclear-localized transcriptional regulators.

1 Plant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
2 Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093, USA.
3 Genomic Analysis Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
4 Howard Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.

* To whom correspondence should be addressed. E-mail: ecker{at}salk.edu

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