EIN2 is a central signal transducer in Arabidopsis ethylene responses. Its NRAMP-like N-terminal membrane domain anchors full-length EIN2 to the endoplasmic reticulum, while its large cytosolic C-terminal domain is controlled by the CTR1 kinase. Ethylene relieves CTR1-mediated inhibition, permitting C-terminal processing and signaling in the nucleus and cytoplasmic P-bodies. EIN2 promotes translational repression of EBF1/EBF2 mRNAs and EIN3/EIL1 accumulation, and associates with ENAP1 and chromatin to promote histone acetylation and ethylene-responsive transcription. These activities connect ethylene perception to development and stress responses; the transport or sensing function of the NRAMP-like domain remains unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0035591 signaling adaptor activity | TAS PMID:23132950 CTR1 phosphorylates the central regulator EIN2 to control et... | NEW | Summary: Full-length EIN2 couples ethylene receptor/CTR1 regulation at the ER membrane to downstream nuclear and cytoplasmic signaling through its processed C-terminal domain. Reason: CTR1 binds and phosphorylates EIN2 (PMID:23132950), while activated EIN2 associates with EBF1/2 3' UTRs and P-body proteins EIN5/PABs (PMID:26496607), and with ENAP1 in nuclear signaling (PMID:27694846). Together these support the non-catalytic coordination of signaling partners required by the QuickGO definition of signaling adaptor activity. Supporting Evidence: PMID:23132950 Here we demonstrate that CTR1 interacts with and directly phosphorylates the cytosolic C-terminal domain of EIN2. Mutations that block the EIN2 phosphorylation sites result in constitutive nuclear localization of the EIN2 C terminus, concomitant with constitutive activation of ethylene responses in Arabidopsis. PMID:26496607 Furthermore, we demonstrate that ethylene induces EIN2 to associate with 3' UTRs and target EBF1/2 mRNA to cytoplasmic processing-body (P-body) through interacting with multiple P-body factors, including EIN5 and PABs. PMID:27694846 Both EIN2 and EIN3 interact with a SANT domain protein named EIN2 nuclear associated protein 1 (ENAP1), overexpression of which results in elevation of histone acetylation and enhanced ethylene-inducible gene expression in an EIN2-dependent manner. |
| GO:0001736 establishment of planar polarity | IGI PMID:17084699 Vectorial information for Arabidopsis planar polarity is med... | KEEP AS NON CORE | Summary: The paper supports a genetic contribution of EIN2, together with AUX1 and GNOM, to root epidermal hair positioning and planar polarity through auxin gradient information. Reason: This is a developmental output of ethylene/auxin crosstalk rather than the core molecular role of EIN2. The annotation is supportable, but it should not be treated as a primary function. Supporting Evidence: PMID:17084699 Here, we report that combinatorial action of the auxin influx carrier AUX1, ETHYLENE-INSENSITIVE2 (EIN2) , and GNOM genes mediates the vector for coordinate hair positioning. |
| GO:0002237 response to molecule of bacterial origin | IMP PMID:20592040 Ethylene signaling regulates accumulation of the FLS2 recept... | KEEP AS NON CORE | Summary: flg22-triggered oxidative burst and stomatal immune responses are reduced in ethylene-insensitive mutants including ein2, with reduced FLS2 accumulation in ein2. Reason: EIN2 contributes to MAMP-triggered immune outputs through ethylene signaling, but this is a context-specific downstream role rather than the core function of the gene product. Supporting Evidence: PMID:20592040 The oxidative burst was diminished in ethylene-insensitive mutants. Flagellin Sensitive2 (FLS2) accumulation was reduced in etr1 and ein2, indicating a requirement of ethylene signaling for FLS2 expression. |
| GO:0006970 response to osmotic stress | IMP PMID:17533512 Arabidopsis EIN2 modulates stress response through abscisic ... | KEEP AS NON CORE | Summary: ein2 mutants are hypersensitive to osmotic stress, and EIN2 affects stress marker gene expression through an ABA-linked pathway. Reason: The phenotype is supported, but the evidence places EIN2 as a signaling crosstalk node downstream of ethylene rather than a dedicated osmotic stress factor. Supporting Evidence: PMID:17533512 An Arabidopsis EIN2 null mutant was supersensitive to both salt and osmotic stress conditions. |
| GO:0006979 response to oxidative stress | TAS PMID:10381874 EIN2, a bifunctional transducer of ethylene and stress respo... | KEEP AS NON CORE | Summary: The original cloning paper reports that EIN2-CEND expression restores responsiveness to paraquat-induced oxygen radicals in ein2 mutant plants. Reason: Oxidative-stress responsiveness is a documented pleiotropic output of EIN2 signaling. It should be retained as non-core because the core role is the ethylene signaling transduction mechanism. Supporting Evidence: PMID:10381874 Expression of the EIN2 CEND is sufficient to constitutively activate ethylene responses and restores responsiveness to jasmonic acid and paraquat-induced oxygen radicals to mutant plants. |
| GO:0009408 response to heat | IMP PMID:15923322 Heat stress phenotypes of Arabidopsis mutants implicate mult... | KEEP AS NON CORE | Summary: The heat-stress mutant survey found ethylene signaling mutants, including ein2, to be more defective in basal thermotolerance, especially under high light. Reason: This supports a non-core contribution of ethylene signaling to heat stress tolerance. It does not redefine EIN2 as a heat-specific response factor. Supporting Evidence: PMID:15923322 Ethylene signaling mutants (ein2 and etr1) and reactive oxygen metabolism mutants (vtc1, vtc2, npq1, and cad2) were more defective in basal than acquired thermotolerance, especially under high light. |
| GO:0009651 response to salt stress | IMP PMID:17533512 Arabidopsis EIN2 modulates stress response through abscisic ... | KEEP AS NON CORE | Summary: The study reports EIN2-dependent altered salt-stress sensitivity and altered ABA/stress-marker responses. Reason: The salt phenotype is supported, but it reflects crosstalk between ethylene, ABA, and stress signaling rather than the core biochemical role of EIN2. Supporting Evidence: PMID:17533512 An Arabidopsis EIN2 null mutant was supersensitive to both salt and osmotic stress conditions. |
| GO:0009651 response to salt stress | IMP PMID:21631530 EIN2 regulates salt stress response and interacts with a MA3... | KEEP AS NON CORE | Summary: ein2 mutants show strong salt sensitivity, EIN2-CEND expression suppresses the salt-sensitive phenotype, and EIN3/EIL1 also contribute to salt tolerance. Reason: The salt response role is well supported but is best curated as a non-core physiological output of the ethylene pathway. Supporting Evidence: PMID:21631530 Mutation of EIN2 led to extreme salt sensitivity as revealed by phenotypic and physiological changes, and overexpression of C-terminus of EIN2 suppressed salt sensitivity in ein2-5, indicating that EIN2 is required for salt tolerance. |
| GO:0009723 response to ethylene | IMP PMID:10381874 EIN2, a bifunctional transducer of ethylene and stress respo... | MODIFY | Summary: EIN2 is required for ethylene responsiveness, and EIN2-CEND expression is sufficient to activate ethylene response phenotypes. Reason: The evidence supports the more informative pathway term rather than the broad stimulus-response term. Proposed replacements: ethylene-activated signaling pathway Supporting Evidence: PMID:10381874 Expression of the EIN2 CEND is sufficient to constitutively activate ethylene responses and restores responsiveness to jasmonic acid and paraquat-induced oxygen radicals to mutant plants. |
| GO:0009725 response to hormone | IMP PMID:10381874 EIN2, a bifunctional transducer of ethylene and stress respo... | MODIFY | Summary: EIN2 was cloned as a central ethylene signaling component with additional hormone/stress crosstalk phenotypes. Reason: The broad hormone response term obscures the specific, core role of EIN2 in ethylene-activated signaling. Proposed replacements: ethylene-activated signaling pathway Supporting Evidence: PMID:10381874 Expression of the EIN2 CEND is sufficient to constitutively activate ethylene responses and restores responsiveness to jasmonic acid and paraquat-induced oxygen radicals to mutant plants. |
| GO:0009753 response to jasmonic acid | IMP PMID:10381874 EIN2, a bifunctional transducer of ethylene and stress respo... | KEEP AS NON CORE | Summary: The original EIN2 paper reports that EIN2-CEND restores responsiveness to jasmonic acid in mutant plants. Reason: JA responsiveness is a supported crosstalk phenotype, but the core role of EIN2 remains ethylene signal transduction. Supporting Evidence: PMID:10381874 Expression of the EIN2 CEND is sufficient to constitutively activate ethylene responses and restores responsiveness to jasmonic acid and paraquat-induced oxygen radicals to mutant plants. |
| GO:0009789 positive regulation of abscisic acid-activated signaling pathway | IMP PMID:10899978 Regulation of abscisic acid signaling by the ethylene respon... | KEEP AS NON CORE | Summary: Ethylene signaling positively regulates aspects of ABA action on root growth, while antagonizing ABA action during germination. Reason: PMID:10899978 explicitly supports positive regulation in the root-growth context. Opposite effects during germination do not invalidate this context-specific annotation; retain it as hormone crosstalk outside the central ethylene mechanism. Supporting Evidence: PMID:10899978 In contrast, the ethylene response pathway positively regulates some aspects of ABA action that involve root growth in the absence of ethylene. |
| GO:0009871 jasmonic acid and ethylene-dependent systemic resistance, ethylene mediated signaling pathway | TAS PMID:11418339 Genes controlling expression of defense responses in Arabido... | KEEP AS NON CORE | Summary: Review-based TAS placing EIN2 in the ethylene branch of jasmonate/ethylene-dependent induced systemic resistance (ISR). The term is a context-specific subtype of ethylene-activated signalling, for which EIN2 is the obligate transducer. Reason: PMID:11418339 is a Curr Opin Plant Biol review with no open-access copy (Europe PMC lists no PMC record) and an abstract-only cache entry that does not name EIN2, so the curator's statement was not seen. The annotation is nevertheless clearly correct in kind rather than merely plausible - ISR is mediated by JA and ethylene signalling (PMID:20348432), and EIN2 is required for all canonical ethylene-activated signalling (ACCEPTed core rows in this review). Retained as a defence-context instance of the core pathway, not as a separate core function. Supporting Evidence: PMID:20348432 Induced systemic resistance is mediated by jasmonate (JA) and ethylene (ET) signaling and requires the transcriptional regulator NPR1, a key regulator in salicylic acid (SA) signaling |
| GO:0009873 ethylene-activated signaling pathway | TAS PMID:10381874 EIN2, a bifunctional transducer of ethylene and stress respo... | ACCEPT | Summary: EIN2 was identified as a central ethylene signaling component, and the EIN2 C-terminal domain is sufficient to activate ethylene responses. Reason: Ethylene-activated signaling is the core biological process for EIN2. Supporting Evidence: PMID:10381874 Expression of the EIN2 CEND is sufficient to constitutively activate ethylene responses and restores responsiveness to jasmonic acid and paraquat-induced oxygen radicals to mutant plants. |
| GO:0009926 auxin polar transport | IMP PMID:9032965 Genetic analysis of the effects of polar auxin transport inh... | KEEP AS NON CORE | Summary: pir2, allelic to ein2, confers resistance to the auxin polar transport inhibitors NPA and TIBA in root elongation. Independent radiolabelled-IAA transport assays (Negi et al. 2008) show that ein2-5 roots have reduced acropetal IAA transport that is no longer regulated by ACC, consistent with EIN2 acting upstream of auxin transport through ethylene-regulated (AUX1-dependent) responses. Reason: PMID:9032965 (Plant Cell Physiol 1996) is abstract-only in the cache, and its abstract itself argues that the root-elongation effect of NPA is not explained by blockage of auxin transport, so the accessible part of the original source does not show an EIN2 effect on transport. The acts_upstream_of_or_within relation is nevertheless independently supported by direct transport measurements in PMID:18363780 (open access), where ein2-5 has less acropetal IAA transport that no longer responds to ACC, and the ethylene effect operates via AUX1-mediated IAA uptake. EIN2 is not a transporter; it acts upstream of auxin transport via ethylene-regulated responses, so this is a non-core downstream output of ethylene signalling. Supporting Evidence: PMID:18363780 ein2-5 and etr1-3 have less acropetal IAA transport, and transport is no longer regulated by ACC. PMID:18363780 which is consistent with ethylene altering AUX1-mediated IAA uptake, and thereby blocking lateral root formation. PMID:9032965 the hypothesis that the inhibitory effect of NPA on root elongation is due to high-level accumulation of auxin as a result of blockage of auxin transport is not applicable to A. thaliana |
| GO:0010087 phloem or xylem histogenesis | IMP PMID:23166504 Plant vascular cell division is maintained by an interaction... | KEEP AS NON CORE | Summary: Ethylene signaling interacts with PXY/CLE41 signaling and ERF factors to maintain vascular cell division and vascular development. Reason: The vascular-development role is supported, but it is a developmental output of the ethylene pathway rather than EIN2's core function. Supporting Evidence: PMID:23166504 Furthermore, blocking ethylene signalling using a variety of ethylene insensitive mutants such as ein2 enhances the cell division defect of pxy. |
| GO:0010119 regulation of stomatal movement | IMP PMID:16961732 Ethylene-induced stomatal closure in Arabidopsis occurs via ... | KEEP AS NON CORE | Summary: ein2 stomata fail to close in response to ethylene or hydrogen peroxide in the guard-cell pathway described in the paper. Reason: This is a supported guard-cell physiological output of ethylene signaling, not the central molecular function of EIN2. Supporting Evidence: PMID:16961732 Stomata of the ethylene signalling ein2-1 and arr2 mutants do not close in response to either ethylene or H(2)O(2) but do generate H(2)O(2) following ethylene challenge. |
| GO:0010150 leaf senescence | IMP PMID:19229035 Trifurcate feed-forward regulation of age-dependent cell dea... | KEEP AS NON CORE | Summary: EIN2 regulates the age-dependent miR164/ORE1 feed-forward circuit and contributes to aging-induced cell death in leaves. Reason: Leaf senescence is a well-supported developmental consequence of EIN2 signaling, but it is not the core mechanistic role of the protein. Supporting Evidence: PMID:19229035 ORE1 expression is up-regulated concurrently with leaf aging by EIN2 but is negatively regulated by miR164. miR164 expression gradually decreases with aging through negative regulation by EIN2, which leads to the elaborate up-regulation of ORE1 expression. However, EIN2 still contributes to aging-induced cell death in the absence of ORE1. |
| GO:0010182 sugar mediated signaling pathway | TAS PMID:12663220 Sugar and hormone connections. | KEEP AS NON CORE | Summary: Sugar-hormone cross-talk review (TAS). Independent primary studies place EIN2 in glucose signalling - ein2 mutants are glucose-oversensitive (glo), and glucose-activated TOR kinase directly phosphorylates EIN2 to block its nuclear localization, with glucose-TOR transcriptional reprogramming largely compromised in ein2-5. Reason: PMID:12663220 is a Trends Plant Sci review cached abstract-only, and the abstract does not name EIN2, so the curator's EIN2-specific statement was not seen. The annotation is independently supported by primary evidence - the glo phenotype of ein2 (PMID:14523448) and direct TOR phosphorylation of EIN2 downstream of glucose (PMID:33658715) - which is consistent with the acts_upstream_of_or_within qualifier. Sugar signalling is a cross-talk role of EIN2 that is decoupled from canonical ethylene-CTR1-EIN2 signalling, not its core ethylene-transducing function, so it is kept as non-core. Supporting Evidence: PMID:14523448 The ethylene-insensitive etr1 and ein2 mutants have glo phenotypes PMID:33658715 Glucose-activated TOR kinase directly phosphorylates EIN2 to prevent its nuclear localization. PMID:33658715 the rapid global transcriptional reprogramming that is directed by glucose-TOR signalling is largely compromised in the ein2-5 mutant |
| GO:0031348 negative regulation of defense response | IMP PMID:16732289 Conserved requirement for a plant host cell protein in powde... | KEEP AS NON CORE | Summary: IMP annotation from a study of mlo-based powdery mildew resistance. Independent studies show that loss of EIN2 or of the downstream EIN3/EIL1 transcription factors enhances resistance in some pathosystems (e.g. ein2-1 against Fusarium graminearum; EIN3/EIL1 repress SID2 to dampen PAMP-triggered immunity). Reason: PMID:16732289 (Nat Genet 2006) is abstract-only in the cache, and the cached abstract states that mlo resistance does not involve ethylene signalling, so the EIN2-specific experiment behind this IMP is in the uncached full text; we defer to the curator, who read it. A negative role of the EIN2 pathway in some defence responses is independently corroborated - ein2-1 shows enhanced resistance to F. graminearum (PMID:31819723), and EIN3/EIL1 downstream of EIN2 negatively regulate PAMP-triggered immunity via SID2 (PMID:19717619). EIN2 also positively regulates other defences (necrotroph resistance, ISR; see the defence-response rows in this review), so the role is context-dependent and a downstream output of ethylene signalling rather than a core function. Supporting Evidence: PMID:31819723 both ein2-1 and ein3-1 mutants showed enhanced disease resistance against F. graminearum PMID:19717619 Taken together, our data provide evidence that EIN3/EIL1 directly target SID2 to downregulate PAMP defenses. PMID:16732289 Epistasis analysis showed that mlo resistance in A. thaliana does not involve the signaling molecules ethylene, jasmonic acid or salicylic acid |
| GO:0042742 defense response to bacterium | IMP PMID:19095898 Glucosinolate metabolites required for an Arabidopsis innate... | KEEP AS NON CORE | Summary: The paper shows that ethylene-dependent pathways are required for pathogen-triggered callose deposition and glucosinolate-linked innate immune responses. Reason: Bacterial defense is a supported downstream immune role of the ethylene pathway but is not EIN2's core molecular function. The accessible source supports the ethylene pathway and callose context; the EIN2-specific mutant assignment is retained with deference to the experimental curator, not claimed to have been independently verified from the partial cache. Supporting Evidence: PMID:19095898 Transcriptional and metabolic profiling in Arabidopsis mutants, coupled with the monitoring of pathogen-triggered callose deposition, have identified major roles in pathogen response for the plant hormone ethylene and the secondary metabolite 4-methoxy-indol-3-ylmethylglucosinolate. |
| GO:0048765 root hair cell differentiation | IGI PMID:17084699 Vectorial information for Arabidopsis planar polarity is med... | KEEP AS NON CORE | Summary: Combined AUX1, EIN2 and GNOM activity positions the root hair initiation site and ROP proteins during root epidermal differentiation. Reason: PMID:17084699 directly demonstrates hair positioning, a specialized feature acquired by root hair cells. The GO:0048765 definition encompasses acquisition of specialized root-hair features; absence of a cell-fate assay alone does not justify the previous over-annotation judgment. Retain this developmental role as non-core. Supporting Evidence: PMID:17084699 Here, we report that combinatorial action of the auxin influx carrier AUX1, ETHYLENE-INSENSITIVE2 (EIN2) , and GNOM genes mediates the vector for coordinate hair positioning. |
| GO:0050832 defense response to fungus | IMP PMID:17513501 ABA is an essential signal for plant resistance to pathogens... | MODIFY | Summary: The study analyzes defense against Pythium irregulare, an oomycete pathogen, and reports roles for JA, ethylene, and ABA defense pathways. Reason: The original study explicitly identifies Pythium irregulare as an oomycete; QuickGO confirms GO:0002229 describes protective responses to oomycetes. This taxonomic correction does not question the curated EIN2 mutant evidence, which is not reproduced in the partial cached full text. Proposed replacements: defense response to oomycetes Supporting Evidence: PMID:17513501 Analyses of Arabidopsis thaliana defense response to the damping-off oomycete pathogen Pythium irregulare show that resistance to P. irregulare requires a multicomponent defense strategy. |
| GO:0050832 defense response to fungus | IMP PMID:19889874 Disruption of poly(ADP-ribosyl)ation mechanisms alters respo... | KEEP AS NON CORE | Summary: IMP annotation from a study of poly(ADP-ribosyl)ation and Botrytis defence. The full text (PMC2799362, read for this review) uses ein2-1 as a hypersusceptible comparator in its Botrytis cinerea disease assays (Fig. 5); ein2 is also required for flg22-induced immunity to Botrytis. Reason: The full text of PMID:19889874 was read via PMC (PMC2799362; the cache entry is abstract-only). Its Results report that parg mutant susceptibility to B. cinerea was not as severe as that of ein2-1 mutant plants, which are known to be hypersusceptible to this fungus (Fig. 5, disease severity scored for Col, parg1-1, parg2-1 and ein2-1). This directly supports the IMP. Independently, flg22-induced PTI to B. cinerea requires EIN2 (PMID:21862710). Defence against necrotrophic fungi is a well-established ethylene-dependent output of EIN2, but not its core molecular role. Supporting Evidence: PMID:21862710 Genetic analysis revealed flg22-induced PTI to Botrytis cinerea requires BIK1, EIN2, and HUB1 but not genes involved in salicylate (SA) functions. |
| GO:0051301 cell division | IMP PMID:23166504 Plant vascular cell division is maintained by an interaction... | KEEP AS NON CORE | Summary: Blocking EIN2-dependent ethylene signaling enhances the vascular cell division defect of pxy mutants. Reason: PMID:23166504 explicitly measures a cell-division phenotype in developing vascular tissue. Tissue specificity does not make the broader cell division process false, and replacing it with histogenesis would discard the experimentally demonstrated process. Retain as a non-core developmental output. Supporting Evidence: PMID:23166504 Furthermore, blocking ethylene signalling using a variety of ethylene insensitive mutants such as ein2 enhances the cell division defect of pxy. |
| GO:0052544 defense response by callose deposition in cell wall | IMP PMID:19095898 Glucosinolate metabolites required for an Arabidopsis innate... | KEEP AS NON CORE | Summary: Pathogen-triggered callose deposition requires ethylene-dependent signaling in the cited innate immune response study. Reason: This is a supported immune output of EIN2-dependent ethylene signaling, but it is not a primary function of EIN2. The accessible source supports the ethylene pathway and callose context; the EIN2-specific mutant assignment is retained with deference to the experimental curator, not claimed to have been independently verified from the partial cache. Supporting Evidence: PMID:19095898 Transcriptional and metabolic profiling in Arabidopsis mutants, coupled with the monitoring of pathogen-triggered callose deposition, have identified major roles in pathogen response for the plant hormone ethylene and the secondary metabolite 4-methoxy-indol-3-ylmethylglucosinolate. |
| GO:0106167 extracellular ATP signaling | IMP PMID:30630869 Extracellular ATP Shapes a Defense-Related Transcriptome Bot... | KEEP AS NON CORE | Summary: ATP-induced defense transcriptome analysis found that many ATP-responsive genes require classical defense hormone pathways including EIN2-dependent ethylene signaling. Reason: EIN2 participates in extracellular ATP defense signaling crosstalk, but this is a non-core downstream pathway context. Supporting Evidence: PMID:30630869 In conclusion, we present a model ( Fig. 10 ) in which ATP binding to P2K1 results in defense gene activation, where more than half of ATP-responsive genes required signaling by one or more of the pathways through EIN2, NPR1, and COI1, but with a more substantial reliance on COI1. |
| GO:0003682 chromatin binding | IDA PMID:28874528 EIN2 mediates direct regulation of histone acetylation in th... | ACCEPT | Summary: EIN2-C associates with chromatin/histone-linked regions through ENAP1 and promotes H3K14Ac/H3K23Ac at ethylene-responsive loci. Reason: Chromatin association is a core nuclear output of cleaved EIN2-C in the ethylene response. Supporting Evidence: PMID:28874528 Chromatin immunoprecipitation followed by deep sequencing (ChIP-seq) and ChIP-reChIP-seq analyses revealed that EIN2-C associates with histone partially through an interaction with EIN2 nuclear-associated protein1 (ENAP1), which preferentially binds to the genome regions that are associated with actively expressed genes both with and without ethylene treatments. |
| GO:0003729 mRNA binding | HDA PMID:27729395 In Planta Determination of the mRNA-Binding Proteome of Arab... | MODIFY | Summary: High-throughput interactome capture supports EIN2 association with polyadenylated mRNA, and targeted ethylene studies show EIN2-CEND binds EBF1/2 3' UTRs. Reason: The original RNA-interactome annotation supports broad mRNA association; its abstract does not identify EIN2 individually. The proposed specialization instead rests on the targeted EIN2 mechanism in PMID:26496607, which explicitly demonstrates association with EBF1/2 3' UTRs. It does not assert that every RNA interaction detected by interactome capture is restricted to a 3' UTR. Proposed replacements: mRNA 3'-UTR binding Supporting Evidence: PMID:26496607 Furthermore, we demonstrate that ethylene induces EIN2 to associate with 3' UTRs and target EBF1/2 mRNA to cytoplasmic processing-body (P-body) through interacting with multiple P-body factors, including EIN5 and PABs. |
| GO:0003729 mRNA binding | IDA PMID:32344669 Discovering the RNA-Binding Proteome of Plant Leaves with an... | MODIFY | Summary: RNA interactome capture in leaves is consistent with mRNA association, and mechanistic ethylene papers identify EBF 3' UTR binding as the relevant EIN2-CEND RNA interaction. Reason: The original RNA-interactome annotation supports broad mRNA association; its abstract does not identify EIN2 individually. The proposed specialization instead rests on the targeted EIN2 mechanism in PMID:26496607, which explicitly demonstrates association with EBF1/2 3' UTRs. It does not assert that every RNA interaction detected by interactome capture is restricted to a 3' UTR. Proposed replacements: mRNA 3'-UTR binding Supporting Evidence: PMID:26496607 Furthermore, we demonstrate that ethylene induces EIN2 to associate with 3' UTRs and target EBF1/2 mRNA to cytoplasmic processing-body (P-body) through interacting with multiple P-body factors, including EIN5 and PABs. |
| GO:0005515 protein binding | IPI PMID:19196655 Interplay between ethylene, ETP1/ETP2 F-box proteins, and de... | REMOVE | Summary: EIN2-CEND physically interacts with ETP1 and ETP2, which mediate EIN2 turnover in the absence of ethylene. Reason: The interaction is biologically important, but the generic protein binding MF is not informative enough for curated functional annotation. Remove the uninformative generic MF annotation while retaining the reported interaction as mechanistic evidence; this decision does not deny that the association occurs. The cited association does not establish a distinct, more informative molecular activity for this row. Supporting Evidence: PMID:19196655 We identified two F-box proteins, EIN2 TARGETING PROTEIN1 (ETP1) and EIN2 TARGETING PROTEIN2 (ETP2), that interact with the EIN2 C-terminal domain (EIN2-CEND), which is highly conserved and sufficient to activate most ethylene responses. |
| GO:0005515 protein binding | IPI PMID:19769567 EIN2, the central regulator of ethylene signalling, is local... | REMOVE | Summary: EIN2 is localized at the ER membrane and specifically interacts with the ethylene receptor ETR1. Reason: The ETR1 interaction should be captured in pathway context, not as vague protein binding. Remove the uninformative generic MF annotation while retaining the reported interaction as mechanistic evidence; this decision does not deny that the association occurs. The cited association does not establish a distinct, more informative molecular activity for this row. Supporting Evidence: PMID:19769567 Here we show, by an integrated approach using in vivo and in vitro fluorescence techniques, that EIN2 is localized at the ER (endoplasmic reticulum) membrane where it shows specific interaction with the ethylene receptor protein ETR1. |
| GO:0005515 protein binding | IPI PMID:21631530 EIN2 regulates salt stress response and interacts with a MA3... | REMOVE | Summary: The study identifies ECIP1 as an EIN2-interacting protein in salt and ethylene response contexts. Reason: The physical interaction is useful evidence but GO:0005515 is too vague to represent EIN2 function. Remove the uninformative generic MF annotation while retaining the reported interaction as mechanistic evidence; this decision does not deny that the association occurs. The cited association does not establish a distinct, more informative molecular activity for this row. Supporting Evidence: PMID:21631530 A MA3 domain-containing protein ECIP1 was further identified to interact with EIN2 in yeast two-hybrid assay and GST pull-down assay. |
| GO:0005515 protein binding | IPI PMID:27694846 EIN2-dependent regulation of acetylation of histone H3K14 an... | REMOVE | Summary: EIN2-CEND interacts with ENAP1 and links ethylene signaling to histone acetylation at ethylene-regulated genes. Reason: This specific interaction supports chromatin/histone regulatory annotations, while generic protein binding adds little functional value. Remove the uninformative generic MF annotation while retaining the reported interaction as mechanistic evidence; this decision does not deny that the association occurs. The cited association does not establish a distinct, more informative molecular activity for this row. Supporting Evidence: PMID:27694846 Both EIN2 and EIN3 interact with a SANT domain protein named EIN2 nuclear associated protein 1 (ENAP1), overexpression of which results in elevation of histone acetylation and enhanced ethylene-inducible gene expression in an EIN2-dependent manner. |
| GO:0042393 histone binding | IDA PMID:28874528 EIN2 mediates direct regulation of histone acetylation in th... | ACCEPT | Summary: EIN2-C associates with histone-containing chromatin through ENAP1 and is required for ethylene-responsive H3K14/H3K23 acetylation. Reason: Histone/chromatin association is a mechanistic nuclear function of activated EIN2-CEND. Supporting Evidence: PMID:28874528 Chromatin immunoprecipitation followed by deep sequencing (ChIP-seq) and ChIP-reChIP-seq analyses revealed that EIN2-C associates with histone partially through an interaction with EIN2 nuclear-associated protein1 (ENAP1), which preferentially binds to the genome regions that are associated with actively expressed genes both with and without ethylene treatments. |
| GO:0046873 metal ion transmembrane transporter activity | IEA GO_REF:0000002 | REMOVE | Summary: EIN2 contains an NRAMP-like membrane domain, but its well-established signaling function does not establish metal transport. Reason: The family-domain association is too broad to establish a transporter role for this signaling protein. UniProt explicitly describes EIN2 as probably not involved in iron uptake, while the primary studies establish receptor/CTR1-controlled signaling. This removal concerns the unsupported electronic transport assignment; it is not proof that all metal sensing or homeostasis roles are absent. Supporting Evidence: PMID:33573082 However, no metal transport activity has been detected in heterologously expressed EIN2 [32], although its possible role as a sensor of divalent metals has been suggested [36]. |
| GO:0006879 intracellular iron ion homeostasis | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: PAINT IBD at the NRAMP node PTN000194431. The inherited assertion rests on NRAMP metal transport, which has not been detected for EIN2. EIN2-dependent ethylene/NO signalling does regulate the iron-acquisition genes FRO2 and IRT1, but that is transcriptional control upstream of the transporters, not the inherited transport-based homeostasis function. Reason: Treated identically to the manganese homeostasis IBA (GO:0030026) from the same node, and consistent with removal of GO:0046873 metal ion transmembrane transporter activity. The entities that execute intracellular iron homeostasis in this context are FRO2/IRT1; EIN2 acts upstream through ethylene signalling (PMID:33573082 "The results obtained clearly support the participation of ET and NO, through EIN2, in the regulation of the Fe acquisition genes FRO2 and IRT1"), which is a regulatory, not a transport-based, contribution. Marked as over-annotation rather than removed because EIN2 does influence iron status indirectly and a divalent-metal sensor role has been suggested. Propagation Review Root cause: PROPAGATION BAD Failure modes: FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000194431 · PTN000194431 SUPPORTS SOURCE BUT NOT TARGET PTHR11706-paint.tsv places the iron and manganese homeostasis IBDs at this NRAMP node, where they rest on the metal-transport activity of NRAMP members. EIN2 retains only the NRAMP-like membrane domain and has no detected metal transport activity; its function has diverged to ER-anchored ethylene signal transduction via the cytosolic C-terminal domain. The node assertion is sound for transporting members but does not transfer to EIN2. Iron and manganese rows are treated identically. Supporting Evidence: PMID:33573082 However, no metal transport activity has been detected in heterologously expressed EIN2 [32], although its possible role as a sensor of divalent metals has been suggested [36]. |
| GO:0009873 ethylene-activated signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro/PANTHER context places EIN2 in an EIN2-specific subfamily, and extensive experimental literature confirms its central role in ethylene-activated signaling. Reason: Although electronically inferred, the annotation matches the core, experimentally established function of EIN2. Supporting Evidence: PMID:10381874 Expression of the EIN2 CEND is sufficient to constitutively activate ethylene responses and restores responsiveness to jasmonic acid and paraquat-induced oxygen radicals to mutant plants. |
| GO:0009873 ethylene-activated signaling pathway | IMP PMID:28874528 EIN2 mediates direct regulation of histone acetylation in th... | ACCEPT | Summary: EIN2-C controls ethylene-responsive histone acetylation and transcriptional activation at ethylene response loci. Reason: This is a core process annotation supported by direct EIN2 pathway evidence. Supporting Evidence: PMID:28874528 Chromatin immunoprecipitation followed by deep sequencing (ChIP-seq) and ChIP-reChIP-seq analyses revealed that EIN2-C associates with histone partially through an interaction with EIN2 nuclear-associated protein1 (ENAP1), which preferentially binds to the genome regions that are associated with actively expressed genes both with and without ethylene treatments. |
| GO:0030001 metal ion transport | IEA GO_REF:0000002 | REMOVE | Summary: EIN2 contains an NRAMP-like membrane domain, but its well-established signaling function does not establish metal transport. Reason: The family-domain association is too broad to establish a transporter role for this signaling protein. UniProt explicitly describes EIN2 as probably not involved in iron uptake, while the primary studies establish receptor/CTR1-controlled signaling. This removal concerns the unsupported electronic transport assignment; it is not proof that all metal sensing or homeostasis roles are absent. Supporting Evidence: PMID:33573082 However, no metal transport activity has been detected in heterologously expressed EIN2 [32], although its possible role as a sensor of divalent metals has been suggested [36]. |
| GO:0030026 intracellular manganese ion homeostasis | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: PAINT IBD at the NRAMP node PTN000194431. The inherited assertion rests on NRAMP metal transport, which has not been detected for EIN2, and there is no EIN2-specific evidence linking it to manganese homeostasis. Reason: Treated identically to the iron homeostasis IBA (GO:0006879) from the same node, and consistent with removal of GO:0046873 metal ion transmembrane transporter activity. EIN2 has diverged from transporting NRAMPs into a signalling protein; the inherited transport-based homeostasis process is an over-annotation for this member, though a divalent-metal sensor role has been suggested and is not excluded. Propagation Review Root cause: PROPAGATION BAD Failure modes: FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000194431 · PTN000194431 SUPPORTS SOURCE BUT NOT TARGET PTHR11706-paint.tsv places the iron and manganese homeostasis IBDs at this NRAMP node, where they rest on the metal-transport activity of NRAMP members. EIN2 retains only the NRAMP-like membrane domain and has no detected metal transport activity; its function has diverged to ER-anchored ethylene signal transduction via the cytosolic C-terminal domain. The node assertion is sound for transporting members but does not transfer to EIN2. Iron and manganese rows are treated identically. Supporting Evidence: PMID:33573082 However, no metal transport activity has been detected in heterologously expressed EIN2 [32], although its possible role as a sensor of divalent metals has been suggested [36]. |
| GO:0040029 epigenetic regulation of gene expression | IMP PMID:28874528 EIN2 mediates direct regulation of histone acetylation in th... | ACCEPT | Summary: EIN2-C regulates H3K14Ac and H3K23Ac at ethylene-responsive loci and promotes rapid transcriptional regulation through ENAP1-associated chromatin. Reason: This is a core nuclear mechanism by which activated EIN2 transduces ethylene signaling to gene expression. Supporting Evidence: PMID:28874528 Chromatin immunoprecipitation followed by deep sequencing (ChIP-seq) and ChIP-reChIP-seq analyses revealed that EIN2-C associates with histone partially through an interaction with EIN2 nuclear-associated protein1 (ENAP1), which preferentially binds to the genome regions that are associated with actively expressed genes both with and without ethylene treatments. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt subcellular mapping is consistent with multiple experimental studies showing ethylene-induced nuclear localization of the cleaved EIN2 C-terminal domain. Reason: Nuclear localization of EIN2-CEND is central to EIN2 signaling. |
| GO:0005634 nucleus | EXP PMID:22936567 Processing and subcellular trafficking of ER-tethered EIN2 c... | ACCEPT | Summary: Ethylene triggers EIN2 dephosphorylation, cleavage, and nuclear translocation of the C-terminal fragment. Reason: The nucleus is a core activated EIN2-CEND location. Supporting Evidence: PMID:22936567 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'). |
| GO:0005634 nucleus | EXP PMID:23070300 Activation of ethylene signaling is mediated by nuclear tran... | ACCEPT | Summary: The cleaved EIN2 carboxyl terminus translocates to the nucleus, where nuclear localization is necessary and sufficient for activating ethylene responses. Reason: This is direct evidence for a core EIN2-CEND cellular location. Supporting Evidence: PMID:23070300 Taken together, these results indicate that ethylene treatment facilitates the translocation of EIN2-GFP from ER membrane into the nucleus. |
| GO:0005634 nucleus | EXP PMID:23132950 CTR1 phosphorylates the central regulator EIN2 to control et... | ACCEPT | Summary: CTR1 phosphorylation prevents signaling, while loss of phosphorylation permits cleavage and nuclear localization of the EIN2 C terminus. Reason: Nuclear localization is a core regulated state of activated EIN2-CEND. Supporting Evidence: PMID:23132950 Here we demonstrate that CTR1 interacts with and directly phosphorylates the cytosolic C-terminal domain of EIN2. Mutations that block the EIN2 phosphorylation sites result in constitutive nuclear localization of the EIN2 C terminus, concomitant with constitutive activation of ethylene responses in Arabidopsis. |
| GO:0005634 nucleus | EXP PMID:25822663 Unsaturation of very-long-chain ceramides protects plant fro... | ACCEPT | Summary: Hypoxia-associated ceramide signaling enhances ER-to-nucleus translocation of EIN2-GFP and stabilization of EIN3-GFP. Reason: The localization is consistent with the established nuclear route of activated EIN2-CEND, even though the hypoxia context is non-core. Supporting Evidence: PMID:25822663 Evidence that C24:1-ceramide interacted with recombinant CTR1 protein and inhibited its kinase activity in vitro, enhanced ER-to-nucleus translocation of EIN2-GFP and stabilization of EIN3-GFP in vivo, suggests a role of ceramides in modulating CTR1-mediated ethylene signaling. |
| GO:0005634 nucleus | EXP PMID:26496607 EIN2-directed translational regulation of ethylene signaling... | ACCEPT | Summary: The translational-regulation study builds on the cleaved EIN2-CEND model and places EIN2-CEND in nuclear and P-body-linked signaling outputs. Reason: The core activated nuclear location is directly corroborated by EIN2 cleavage and trafficking in PMID:22936567. The original translational-regulation paper is not used here as independent proof of nuclear localization from its abstract. Supporting Evidence: PMID:22936567 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'). |
| GO:0005634 nucleus | EXP PMID:26496608 Gene-specific translation regulation mediated by the hormone... | ACCEPT | Summary: EIN2 participates in gene-specific translational regulation while also serving as the hormone-signaling molecule connecting ethylene perception to downstream responses. Reason: The core activated nuclear location is directly corroborated by EIN2 cleavage and trafficking in PMID:22936567. The original translational-regulation paper is not used here as independent proof of nuclear localization from its abstract. Supporting Evidence: PMID:22936567 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'). |
| GO:0005634 nucleus | EXP PMID:26507893 Mitogen-activated protein kinase 6 mediates nuclear transloc... | ACCEPT | Summary: Under methyl jasmonate-induced senescence, MPK6 promotes cleavage and nuclear translocation of ORE3/EIN2 CEND. Reason: This supports nuclear localization of the active C-terminal fragment, although the senescence trigger is a non-core context. Supporting Evidence: PMID:26507893 The C-terminal end of ORE3/EIN2 (CEND) was cleaved from ORE3/EIN2 located in the endoplasmic reticulum and then transferred to the nucleus during MeJA-induced senescence. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | MODIFY | Summary: Cytoplasmic localization is consistent with activated EIN2-CEND foci, but the key mechanistic cytoplasmic compartment is the P-body. Reason: The broad cytoplasm term should be replaced by the more specific P-body location where EIN2-CEND regulates EBF1/2 mRNAs. Proposed replacements: P-body Supporting Evidence: PMID:26496607 Furthermore, we demonstrate that ethylene induces EIN2 to associate with 3' UTRs and target EBF1/2 mRNA to cytoplasmic processing-body (P-body) through interacting with multiple P-body factors, including EIN5 and PABs. |
| GO:0005737 cytoplasm | EXP PMID:23070300 Activation of ethylene signaling is mediated by nuclear tran... | KEEP AS NON CORE | Summary: The paper reports cytoplasmic CEND-GFP signal and cytoplasmic speckles in addition to nuclear localization. Reason: The broad cytoplasmic observation is supported but less specific than the core nuclear and P-body localizations. Supporting Evidence: PMID:23070300 Meanwhile, we also observed that EIN2-GFP formed speckles in cytoplasm apart from nuclear localization |
| GO:0005737 cytoplasm | EXP PMID:25843012 Targeting Plant Ethylene Responses by Controlling Essential ... | KEEP AS NON CORE | Summary: Experimental cytoplasm annotation from a study of EIN2-ETR1 complex formation at the ER. ER-anchored full-length EIN2 and the cleaved EIN2-CEND (cytoplasmic speckles/P-bodies) are both cytoplasmic, so the annotation is clearly correct for EIN2. Reason: PMID:25843012 (Mol Plant 2015) has no open-access copy (Europe PMC lists no PMC record) and the cache is abstract-only, so the specific experiment was not seen. Deferral is justified because the location is independently established - EIN2 is ER-localized (stated in this abstract) and EIN2-GFP forms cytoplasmic speckles (PMID:23070300). Generic cytoplasm is less informative than the ER membrane and P-body locations. Supporting Evidence: PMID:23070300 Meanwhile, we also observed that EIN2-GFP formed speckles in cytoplasm apart from nuclear localization |
| GO:0005737 cytoplasm | EXP PMID:26496607 EIN2-directed translational regulation of ethylene signaling... | MODIFY | Summary: Ethylene induces EIN2-CEND to associate with EBF1/2 3' UTRs and target those mRNAs to cytoplasmic P-bodies. Reason: The evidence supports the more specific P-body location rather than generic cytoplasm. Proposed replacements: P-body Supporting Evidence: PMID:26496607 Furthermore, we demonstrate that ethylene induces EIN2 to associate with 3' UTRs and target EBF1/2 mRNA to cytoplasmic processing-body (P-body) through interacting with multiple P-body factors, including EIN5 and PABs. |
| GO:0005737 cytoplasm | EXP PMID:26496608 Gene-specific translation regulation mediated by the hormone... | MODIFY | Summary: EIN2 mediates gene-specific translational regulation through EBF2 3'UTR machinery, consistent with the P-body translational repression module. Reason: The cytoplasmic signaling site should be captured specifically as P-body when supported by the translational-regulation evidence. Proposed replacements: P-body Supporting Evidence: PMID:26496607 Furthermore, we demonstrate that ethylene induces EIN2 to associate with 3' UTRs and target EBF1/2 mRNA to cytoplasmic processing-body (P-body) through interacting with multiple P-body factors, including EIN5 and PABs. |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular mapping is consistent with direct experimental evidence that full-length EIN2 resides at the ER membrane before ethylene activation. Reason: ER membrane localization is a core feature of full-length EIN2. |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:19769567 EIN2, the central regulator of ethylene signalling, is local... | ACCEPT | Summary: EIN2 is localized at the ER membrane and interacts with the ER-localized ethylene receptor ETR1. Reason: This is direct evidence for the core starting location of EIN2 signaling. Supporting Evidence: PMID:19769567 Here we show, by an integrated approach using in vivo and in vitro fluorescence techniques, that EIN2 is localized at the ER (endoplasmic reticulum) membrane where it shows specific interaction with the ethylene receptor protein ETR1. |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:22936567 Processing and subcellular trafficking of ER-tethered EIN2 c... | ACCEPT | Summary: ER-tethered EIN2 undergoes ethylene-dependent processing and releases a C-terminal fragment that moves to the nucleus. Reason: Full-length EIN2 at the ER membrane is central to the ER-to-nucleus signaling mechanism. Supporting Evidence: PMID:22936567 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'). |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:23070300 Activation of ethylene signaling is mediated by nuclear tran... | ACCEPT | Summary: EIN2-GFP colocalizes with ER markers, and the N-terminal membrane-spanning region accounts for ER localization. Reason: This is direct support for EIN2's core ER membrane localization. Supporting Evidence: PMID:23070300 Taken together, these results indicate that ethylene treatment facilitates the translocation of EIN2-GFP from ER membrane into the nucleus. |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:23132950 CTR1 phosphorylates the central regulator EIN2 to control et... | ACCEPT | Summary: CTR1 phosphorylates ER-associated EIN2, preventing signaling until ethylene perception permits release of the C-terminal domain. Reason: ER membrane localization is required for the upstream receptor/CTR1 regulation of EIN2. Supporting Evidence: PMID:23132950 Here we demonstrate that CTR1 interacts with and directly phosphorylates the cytosolic C-terminal domain of EIN2. Mutations that block the EIN2 phosphorylation sites result in constitutive nuclear localization of the EIN2 C terminus, concomitant with constitutive activation of ethylene responses in Arabidopsis. |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:25822663 Unsaturation of very-long-chain ceramides protects plant fro... | ACCEPT | Summary: The hypoxia study reports modulation of ER-to-nucleus EIN2 trafficking in the ethylene signaling pathway. Reason: The ER membrane state is consistent with the core EIN2 localization model. Supporting Evidence: PMID:25822663 Evidence that C24:1-ceramide interacted with recombinant CTR1 protein and inhibited its kinase activity in vitro, enhanced ER-to-nucleus translocation of EIN2-GFP and stabilization of EIN3-GFP in vivo, suggests a role of ceramides in modulating CTR1-mediated ethylene signaling. |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:25843012 Targeting Plant Ethylene Responses by Controlling Essential ... | ACCEPT | Summary: EIN2 is an ER-localized membrane protein whose C-terminal NLS region also mediates interaction with ETR1. Reason: This supports the core ER membrane localization and receptor-associated signaling context. Supporting Evidence: PMID:25843012 A central element in ethylene signaling is the endoplasmic reticulum (ER)-localized membrane protein ethylene insensitive2 (EIN2). |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: EIN2 is a multi-pass membrane protein, but experimental evidence places the full-length protein specifically at the ER membrane. Reason: The generic membrane term should be replaced by the specific, supported ER membrane location. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: PMID:19769567 Here we show, by an integrated approach using in vivo and in vitro fluorescence techniques, that EIN2 is localized at the ER (endoplasmic reticulum) membrane where it shows specific interaction with the ethylene receptor protein ETR1. |
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Download this section (compressed HTML)Q: What protease or protease complex directly cleaves EIN2-CEND during ethylene signaling, and is the same processing machinery used during methyl jasmonate- or hypoxia-triggered EIN2 activation?
Suggested experts: Hong Qiao, Joseph R. Ecker, Hongwei Guo
Q: Does the NRAMP-like N-terminal domain of EIN2 retain any ion transport or ion-sensing activity, or is it a structurally repurposed membrane-tethering module in the EIN2 subfamily?
Suggested experts: Joseph R. Ecker, Chi-Kuang Wen
Experiment: Express full-length EIN2 and N-terminal EIN2 membrane-domain constructs in a transporter-deficient yeast or plant heterologous assay alongside Arabidopsis NRAMP positive controls; measure manganese and iron transport, localization, and ethylene-pathway complementation separately.
Hypothesis: EIN2's NRAMP-like membrane domain is not an active metal transporter in planta.
Type: heterologous transport assay
Experiment: Generate endogenous EIN2 separation-of-function alleles that selectively disrupt ENAP1/chromatin association or EBF1/2 3'UTR/P-body association, then compare histone acetylation, EBF translation, EIN3 stabilization, and ethylene response phenotypes.
Hypothesis: EIN2 nuclear chromatin regulation and P-body translational repression are separable outputs of the cleaved C-terminal domain.
Type: endogenous allele engineering and multi-omic phenotyping
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