POLARIS is a copper-binding peptide that interacts with ETR1 to negatively regulate ethylene signaling in Arabidopsis

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via two cysteine residues conserved in the related species Camelina sativa. These residues are also essential for biological function. This affinity precludes a role for PLS as a cytosolic Cu chaperone. We demonstrate that PLS localizes to endomembranes and interacts with the transmembrane domain of the receptor protein ETR1. PLS-ETR1 binding is increased in the presence of copper, and this interaction provides a Cu-dependent mechanism for mediating the repression of ethylene responses. Because PLS transcription is upregulated by auxin and downregulated by ethylene, PLS-ETR1 interactions also provide a mechanism for modulation of ethylene responses in high-auxin tissues.

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