text: Two proteins are crucial for interacting ethylene with the receptors, namely constitutive triple response 1 (CTR1) and ethylene insensitive 2 (EIN2). CTR1 is a serine/threonine protein kinase that functions as a negative regulator of ethylene signalling. It is a member of the signaling protein mitogen-activated protein kinase (MAPK) kinase kinase. EIN2 is required for ethylene signalling and is part of the NRAMP (natural resistance-associated macrophage protein) family of metal transporters; it comprises a large, N-terminal portion containing multiple transmembrane domains (EIN2-N) in the ER membrane and a cytosolic C-terminal portion (EIN2-C). Other proteins such as reversion to ethylene sensitivity 1 (RTE1), cytochrome b5 and tetratricopeptide repeat protein 1 (TRP1) also play important roles in ethylene signaling. RTE1 is a highly conserved proteins in plants and protists but absent in fungi and prokaryotes. TRP1 is genetically related to transmembrane and coiled-coil protein 1 (TCC1) in animals that is involved F actin function and competes with Raf-1 for Ras binding.
  Unlike in most signal transductions where the ligands activate their receptors to relay their signals, ethylene acts as the suppressor of its receptor, and the receptor being the negative regulator in ethylene responses. Ethylene receptor is active in the absence of ethylene. Without ethylene, the receptor binds to CTR1 at its C-terminal kinase domain. The kinase activity of CTR1 becomes activated and phosphorylates the neighbouring EIN2. As long as EIN2 remains highly phosphorylated, it remains inactive and there never is an ethylene signal relay. In ETR1, the receptor histidine kinase is required for binding with EIN2. RTE1 can bind to and activate ETR1 independent of CTR1. There is evidence that cytochrome b5 aids or acts similar to RTE1.
  Ethylene binding to the receptor disrupts the EIN2 phosphorylation. It does not cause any particular change in the structural feature of the receptor-CTR1-EIN2 complex or stop the phosphorylation. In fact, at low level of ethylene there is increased receptor-CTR1-EIN2 complexes, which is then reduced as ethylene level rises. The turnover process is not yet fully understood. The only consequence of ethylene binding is reduced phosphorylation of EIN2. Under such condition EIN2 is activated and is cleaved to release EIN2-C from the membrane-bound EIN2-N portion. The enzyme that causes the cleavage is yet unknown. The role of EIN2-N is also unknown in A. thaliana. But in rice, its homologue OsEIN2-N (Os for Oryza sativa, the scientific name for rice) interacts with another protein, mao huzi 3 (MHZ3), a mutation of which gives rise to insensitivity to ethylene.
  EIN2-C is the main component that mediates ethylene signal in the cell. It acts in two ways. In one, it binds the mRNAs that encode for EIN3-binding F-box proteins, EBF1 and EBF2 to cause their degradation. In another, it enters the nucleus to bind with EIN2 nuclear associated protein 1 (ENAP1) to regulate transcriptional and translational activities of EIN3 and the related EIL1 transcription factor to cause most of the ethylene responses.