Hormone signaling must necessarily start with the receptor and intuitively, it is logical that a receptor would be a key point of regulation. The ethylene receptor ETR1 was the first protein to be unambiguously identified as a phytohormone receptor. It was also the first protein with homology to His kinases to be identified in a higher eukaryote (Chang et al., 1993 ). ETR1 is homologous to the prokaryotic family of signal transducers known as two-component regulators. Mutant alleles of ETR1 confer dominant ethylene insensitivity. It functions as a dimer and exhibits copper-mediated high affinity ethylene binding (for review, see Bleecker and Kende, 2000 ). ETR1 is a member of a family of five proteins (ETR1, ETR2, EIN4, ERS1, and ERS2). These receptors can be structurally separated into three domains briefly summarized as follows: The sensor domain contains three hydrophobic, putative transmembrane stretches. Ethylene binding occurs within this amino terminal hydrophobic region and all of the known ETR1 mutations are located within this portion of the protein. Three of the receptors, EIN4, ETR2 and ERS2 are predicted to have a fourth membrane-spanning domain. The amino terminal domain mediates dimerization and copper binding. The GAF domain, which is conserved among
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