Processing and subcellular trafficking of ER-tethered EIN2 control response to ethylene gas

Hong Qiao, Zhouxin Shen, Shao Shan Carol Huang, Robert J. Schmitz, Mark A. Urich, Steven P. Briggs, Joseph R. Ecker

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)390-393
Number of pages4
JournalScience
Volume338
Issue number6105
DOIs
StatePublished - Oct 19 2012

ASJC Scopus subject areas

  • General

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