ERECTA (ER) is a plasma-membrane leucine-rich-repeat receptor-like serine/threonine kinase (LRR-RLK) with an extracellular domain of 20 LRRs, a single transmembrane segment and a cytoplasmic kinase domain. With its paralogs ERL1 and ERL2 it forms the ERECTA family (ERf), which perceives secreted cysteine-rich EPF/EPFL peptides. In the leaf epidermis ERECTA is the principal receptor for EPF2: MEPF2 binds the ERECTA ectodomain within a constitutive complex with the receptor-like co-receptor TOO MANY MOUTHS (TMM), ligand binding recruits SERK co-receptor kinases (BAK1/SERK3 and others) with which ERECTA transphosphorylates, and the signal is relayed through the MAPKKK YODA and MKK4/MKK5 to MPK3/MPK6, which phosphorylate and destabilize the stomatal-entry bHLH SPEECHLESS. ERECTA signalling thereby limits stomatal lineage entry, while the antagonistic peptide stomagen/EPFL9 competes for the same receptor. In shoot organs, ERECTA perceives EPFL4/EPFL6 from the endodermis/phloem and, through the same YODA-MKK4/5-MPK3/6 module, promotes localized cell proliferation that determines inflorescence architecture, pedicel and internode elongation and organ shape. ERECTA additionally contributes to transpiration efficiency, thermotolerance, vascular and ovule development, and quantitative resistance to some bacterial and fungal pathogens.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001558 regulation of cell growth | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT inference of regulation of cell growth for the ERECTA clade (seeded by ERECTA and rice orthologs). Reason: ERECTA signalling promotes localized cell proliferation and expansion in stems, pedicels and lateral organs; the inference is sound but describes a downstream growth output rather than the receptor's core activity. Supporting Evidence: PMID:16126863 Both genetic and cellular analyses indicate that auxin and the ER pathway regulate cell division and cell expansion in a largely independent but overlapping manner during elaboration of inflorescence architecture. |
| GO:0001558 regulation of cell growth | IGI PMID:16126863 Interaction of auxin and ERECTA in elaborating Arabidopsis i... | KEEP AS NON CORE | Summary: Genetic interaction of ERECTA with auxin (YUCCA5 activation tag) in inflorescence architecture. Reason: Valid regulatory output of ERECTA signalling in organ growth; non-core. Supporting Evidence: PMID:16126863 Both genetic and cellular analyses indicate that auxin and the ER pathway regulate cell division and cell expansion in a largely independent but overlapping manner during elaboration of inflorescence architecture. |
| GO:0001558 regulation of cell growth | IMP PMID:16007076 The ERECTA gene regulates plant transpiration efficiency in ... | KEEP AS NON CORE | Summary: erecta mutants alter epidermal cell expansion and mesophyll proliferation affecting transpiration efficiency. Reason: Growth effects are downstream outputs of ERECTA receptor signalling; non-core. Supporting Evidence: PMID:16007076 Mechanisms include, but are not limited to, effects on stomatal density, epidermal cell expansion, mesophyll cell proliferation and cell-cell contact. |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro protein kinase domain mapping. Reason: ERECTA has an active cytoplasmic Ser/Thr kinase domain; correct but general. Supporting Evidence: PMID:26320950 SERK and ERECTA family RLKs transphosphorylate each other. |
| GO:0004674 protein serine/threonine kinase activity | IDA DOI:10.1046/j.1469-8137.2001.00150.x | ACCEPT | Summary: In vitro kinase activity of the ERECTA cytoplasmic domain (Lease et al. 2001, New Phytologist). Reason: The publication is not cached, but ERECTA Ser/Thr kinase activity is independently supported by its transphosphorylation with SERK kinases and by the requirement of its kinase domain for function; accepted, deferring to the curator. Supporting Evidence: PMID:26320950 SERK and ERECTA family RLKs transphosphorylate each other. |
| GO:0004674 protein serine/threonine kinase activity | IEA GO_REF:0000003 | ACCEPT | Summary: EC 2.7.11.1 mapping to protein serine/threonine kinase activity. Reason: Consistent with experimental evidence. |
| GO:0005102 signaling receptor binding | IPI PMID:28536146 A receptor-like protein acts as a specificity switch for the... | ACCEPT | Summary: ERECTA binds the co-receptor TMM (Q9SSD1). Reason: ERECTA and TMM form constitutive receptor complexes that together recognize EPF1/EPF2; association with this signalling receptor is a genuine, informative interaction for the receptor complex. Supporting Evidence: PMID:28536146 Here we show that TMM and ER or ER-LIKE1 (ERL1) form constitutive complexes, which recognize EPF1 and EPF2, but the single ERfs do not. |
| GO:0005515 protein binding | IPI PMID:26083750 Competitive binding of antagonistic peptides fine-tunes stom... | MODIFY | Summary: ERECTA binds the stomagen/EPFL9 peptide (Q9SV72). Reason: Direct binding of a peptide ligand to the ERECTA ectodomain; peptide binding is the informative term (also annotated separately from the same paper). Proposed replacements: peptide binding Supporting Evidence: PMID:26083750 Stomagen peptide competitively replaced EPF2 binding to ER. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005515 protein binding | IPI PMID:29320478 An extracellular network of Arabidopsis leucine-rich repeat ... | REMOVE | Summary: Binary interactions of the ERECTA ectodomain with other LRR-RK ectodomains in a high-throughput extracellular interaction screen. Reason: Generic protein binding is uninformative. These are ectodomain-ectodomain interactions from a large-scale in vitro network screen; individual partners (other than the SERK co-receptors, which are captured by receptor serine/threonine kinase binding) lack functional characterization with ERECTA. Removal does not imply that the interactions are false. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding inferred from the kinase domain. Reason: Required for kinase catalysis; correct. |
| GO:0005739 mitochondrion | HDA PMID:14671022 Experimental analysis of the Arabidopsis mitochondrial prote... | MARK AS OVER ANNOTATED | Summary: ERECTA peptides detected in an LC-MS/MS proteome of isolated mitochondria. Reason: ERECTA is a signal-peptide-bearing single-pass transmembrane receptor kinase repeatedly localized to the plasma membrane with functional fluorescent fusions. A mitochondrial assignment from organelle proteomics most likely reflects co-purifying membranes and does not represent a site of ERECTA function. Supporting Evidence: PMID:26203655 Functional ERECTA-YFP protein driven by its own promoter (ERECTApro::ERECTA-YFP) showed uniform signals in the plasma membrane of nearly all protodermal cells |
| GO:0005886 plasma membrane | EXP PMID:22241782 Direct interaction of ligand-receptor pairs specifying stoma... | ACCEPT | Summary: Functional epitope-tagged ERECTA in membrane fractions; receptor for apoplastic EPF peptides. Reason: Plasma membrane is the site of ERECTA ligand perception and signalling. Supporting Evidence: PMID:22241782 The epitope-tagged TMM, ERECTA, and ERL1 were detected in membrane (microsomal) fractions, consistent with their predicted subcellular localizations |
| GO:0005886 plasma membrane | IDA PMID:26203655 Molecular Framework of a Regulatory Circuit Initiating Two-D... | ACCEPT | Summary: ERECTA-YFP localizes to the plasma membrane of protodermal cells. Reason: Direct imaging of a functional fusion. Supporting Evidence: PMID:26203655 Functional ERECTA-YFP protein driven by its own promoter (ERECTApro::ERECTA-YFP) showed uniform signals in the plasma membrane of nearly all protodermal cells |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular location mapping. Reason: Consistent with experimental data. |
| GO:0005886 plasma membrane | ISM GO_REF:0000122 | ACCEPT | Summary: Sequence-model prediction of plasma membrane localization. Reason: Consistent with experimental data. |
| GO:0005886 plasma membrane | NAS PMID:8624444 The Arabidopsis ERECTA gene encodes a putative receptor prot... | ACCEPT | Summary: Predicted receptor topology in the original ERECTA cloning paper. Reason: Confirmed by later imaging and fractionation. Supporting Evidence: PMID:8624444 The deduced ER protein contains a cytoplasmic protein kinase catalytic domain, a transmembrane region, and an extracellular domain consisting of leucine-rich repeats |
| GO:0009664 plant-type cell wall organization | IMP PMID:19589071 The ERECTA Receptor-Like Kinase Regulates Cell Wall-Mediated... | KEEP AS NON CORE | Summary: erecta mutants have altered cell-wall composition linked to fungal resistance. Reason: An indirect consequence of ERECTA signalling relevant to immunity; non-core. Supporting Evidence: PMID:19589071 Analyses of er cell walls revealed that total neutral sugars were reduced and uronic acids increased relative to those of wild-type walls. |
| GO:0009944 polarity specification of adaxial/abaxial axis | IMP PMID:12874130 Novel as1 and as2 defects in leaf adaxial-abaxial polarity r... | KEEP AS NON CORE | Summary: ERECTA enhances as1/as2 leaf polarity defects. Reason: Genetic modifier role in leaf adaxial identity in a sensitized background; non-core. Supporting Evidence: PMID:12874130 We provide genetic evidence that the Arabidopsis ERECTA (ER) gene is involved in the AS1-AS2 pathway to promote leaf adaxial fate. |
| GO:0009965 leaf morphogenesis | IMP PMID:16007076 The ERECTA gene regulates plant transpiration efficiency in ... | KEEP AS NON CORE | Summary: erecta alters leaf anatomy and morphology. Reason: Organ-shape output of ERECTA signalling; non-core but valid. Supporting Evidence: PMID:16007076 Mechanisms include, but are not limited to, effects on stomatal density, epidermal cell expansion, mesophyll cell proliferation and cell-cell contact. |
| GO:0010087 phloem or xylem histogenesis | IMP PMID:23578929 WOX4 and WOX14 act downstream of the PXY receptor kinase to ... | KEEP AS NON CORE | Summary: er enhances pxy vascular organization defects. Reason: Genetic interaction in vascular patterning; non-core. Supporting Evidence: PMID:23578929 much more striking changes in the shape of vascular bundles were observed in pxy er double mutants |
| GO:0010103 stomatal complex morphogenesis | IEA GO_REF:0000117 | MODIFY | Summary: ARBA prediction of stomatal complex morphogenesis. Reason: ERECTA's role in the stomatal lineage is as the EPF2 receptor that inhibits stomatal lineage entry and, with its paralogs, enforces stomatal patterning; 'morphogenesis' mis-describes this regulatory role. Proposed replacements: negative regulation of stomatal complex development |
| GO:0010103 stomatal complex morphogenesis | IMP PMID:16002616 Stomatal patterning and differentiation by synergistic inter... | MODIFY | Summary: ER-family triple mutants have clustered stomata; synergy with tmm. Reason: The genetic evidence shows that ERECTA-family receptors restrict stomatal lineage entry and enforce patterning, i.e. they negatively regulate stomatal development; this is the more accurate term. Proposed replacements: negative regulation of stomatal complex development Supporting Evidence: PMID:16002616 Loss-of-function mutations in all three ER-family genes cause stomatal clustering. |
| GO:0010148 transpiration | IMP PMID:16007076 The ERECTA gene regulates plant transpiration efficiency in ... | KEEP AS NON CORE | Summary: ERECTA underlies a QTL for transpiration efficiency. Reason: Physiological consequence of ERECTA effects on stomatal density and leaf anatomy; non-core. Supporting Evidence: PMID:16007076 Here we report the isolation of a gene that regulates transpiration efficiency, ERECTA. |
| GO:0010286 heat acclimation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT inference of heat acclimation from Arabidopsis and rice ERECTA. Reason: ERECTA contributes to thermotolerance (er mutants are heat hypersensitive); a genuine but secondary role. Supporting Evidence: PMID:26280413 Arabidopsis er mutants are hypersensitive to heat |
| GO:0016020 membrane | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of membrane localization. Reason: Correct; plasma membrane is the specific location. |
| GO:0019199 transmembrane receptor protein kinase activity | ISS PMID:8624444 The Arabidopsis ERECTA gene encodes a putative receptor prot... | ACCEPT | Summary: Sequence similarity-based assignment of transmembrane receptor protein kinase activity. Reason: Core activity, now experimentally supported (ligand binding to the ectodomain and kinase transphosphorylation with SERKs). The more specific transmembrane receptor protein serine/threonine kinase activity is used in core functions. Supporting Evidence: PMID:8624444 The deduced ER protein contains a cytoplasmic protein kinase catalytic domain, a transmembrane region, and an extracellular domain consisting of leucine-rich repeats PMID:22241782 Here we report the direct, robust, and saturable binding of bioactive EPF peptides to the ERECTA family. |
| GO:0030155 regulation of cell adhesion | IMP PMID:16007076 The ERECTA gene regulates plant transpiration efficiency in ... | KEEP AS NON CORE | Summary: erecta affects cell-cell contact in leaves. Reason: Reported as an anatomical correlate of transpiration-efficiency differences; mechanism unclear and indirect. Supporting Evidence: PMID:16007076 Mechanisms include, but are not limited to, effects on stomatal density, epidermal cell expansion, mesophyll cell proliferation and cell-cell contact. |
| GO:0033612 receptor serine/threonine kinase binding | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of receptor serine/threonine kinase binding (ERECTA family node). Reason: ERECTA-family receptors form homo- and heteromers and associate with SERK co-receptor kinases. Supporting Evidence: PMID:26320950 EPF ligands induce the heteromerization of ERECTA and SERK family RLKs. |
| GO:0033612 receptor serine/threonine kinase binding | IPI PMID:26320950 Differential Function of Arabidopsis SERK Family Receptor-li... | ACCEPT | Summary: ERECTA associates with SERK1, SERK2, BAK1/SERK3 and SERK4 upon EPF stimulation. Reason: Ligand-induced heteromerization with SERK co-receptor kinases is part of the ERECTA activation mechanism. Supporting Evidence: PMID:26320950 EPF ligands induce the heteromerization of ERECTA and SERK family RLKs. |
| GO:0033612 receptor serine/threonine kinase binding | IPI PMID:26320950 Differential Function of Arabidopsis SERK Family Receptor-li... | ACCEPT | Summary: ERECTA associates with SERK1, SERK2, BAK1/SERK3 and SERK4 upon EPF stimulation. Reason: Ligand-induced heteromerization with SERK co-receptor kinases is part of the ERECTA activation mechanism. Supporting Evidence: PMID:26320950 EPF ligands induce the heteromerization of ERECTA and SERK family RLKs. |
| GO:0033612 receptor serine/threonine kinase binding | IPI PMID:26320950 Differential Function of Arabidopsis SERK Family Receptor-li... | ACCEPT | Summary: ERECTA associates with SERK1, SERK2, BAK1/SERK3 and SERK4 upon EPF stimulation. Reason: Ligand-induced heteromerization with SERK co-receptor kinases is part of the ERECTA activation mechanism. Supporting Evidence: PMID:26320950 EPF ligands induce the heteromerization of ERECTA and SERK family RLKs. |
| GO:0033612 receptor serine/threonine kinase binding | IPI PMID:26320950 Differential Function of Arabidopsis SERK Family Receptor-li... | ACCEPT | Summary: ERECTA associates with SERK1, SERK2, BAK1/SERK3 and SERK4 upon EPF stimulation. Reason: Ligand-induced heteromerization with SERK co-receptor kinases is part of the ERECTA activation mechanism. Supporting Evidence: PMID:26320950 EPF ligands induce the heteromerization of ERECTA and SERK family RLKs. |
| GO:0042277 peptide binding | IPI PMID:26083750 Competitive binding of antagonistic peptides fine-tunes stom... | ACCEPT | Summary: ERECTA directly binds EPF2 and stomagen peptides. Reason: Ligand binding by the LRR ectodomain is part of ERECTA's receptor function. Supporting Evidence: PMID:26083750 Both EPF2 and Stomagen directly bind to ER and its co-receptor TOO MANY MOUTHS. |
| GO:0042277 peptide binding | IPI PMID:26083750 Competitive binding of antagonistic peptides fine-tunes stom... | ACCEPT | Summary: ERECTA directly binds EPF2 and stomagen peptides. Reason: Ligand binding by the LRR ectodomain is part of ERECTA's receptor function. Supporting Evidence: PMID:26083750 Both EPF2 and Stomagen directly bind to ER and its co-receptor TOO MANY MOUTHS. |
| GO:0042659 regulation of cell fate specification | IGI PMID:37606225 Epigenetic regulation of female germline development through... | KEEP AS NON CORE | Summary: ERECTA genetically interacts with SWR1/SDG2 to restrict megaspore mother cell fate. Reason: A reproductive developmental role; non-core. Supporting Evidence: PMID:37606225 genetically interact with the ERECTA (ER) receptor kinase signaling pathway and regulate female germline development by restricting the MMC cell fate to a single cell in the ovule primordium |
| GO:0042742 defense response to bacterium | IMP PMID:14617092 ERECTA, an LRR receptor-like kinase protein controlling deve... | KEEP AS NON CORE | Summary: ERECTA underlies the QRS1 resistance locus to Ralstonia solanacearum. Reason: Genuine quantitative contribution to bacterial wilt resistance; non-core relative to developmental signalling. Supporting Evidence: PMID:14617092 Susceptible Ler plants transformed with a wild-type ERECTA gene, and the LER line showed increased disease resistance to R. solanacearum |
| GO:0048281 inflorescence morphogenesis | IMP PMID:11910003 KNAT1 and ERECTA regulate inflorescence architecture in Arab... | ACCEPT | Summary: ERECTA with KNAT1 regulates inflorescence architecture. Reason: Inflorescence architecture (compact inflorescence, short pedicels) is the classic erecta phenotype and reflects ERECTA signalling via YODA-MKK4/5-MPK3/6 promoting localized cell proliferation; this is one of ERECTA's two principal developmental roles. Supporting Evidence: PMID:23263767 suggesting that the MPK3/MPK6 cascade functions downstream of the ER receptor |
| GO:0048827 phyllome development | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA prediction of phyllome development. Reason: ERECTA influences leaf and floral organ shape; general but not wrong. |
| GO:0050832 defense response to fungus | IMP PMID:15998304 ERECTA receptor-like kinase and heterotrimeric G protein fro... | KEEP AS NON CORE | Summary: ERECTA corresponds to the QRP1 locus for resistance to Plectosphaerella cucumerina. Reason: Genuine immunity contribution; non-core. Supporting Evidence: PMID:15998304 QRP1, the locus showing the strongest effect, was found to correspond to the ERECTA (ER) gene |
| GO:0051302 regulation of cell division | IGI PMID:16126863 Interaction of auxin and ERECTA in elaborating Arabidopsis i... | KEEP AS NON CORE | Summary: ERECTA and auxin regulate cell division in inflorescence elaboration. Reason: Output of ERECTA-MAPK signalling in organ growth; non-core. Supporting Evidence: PMID:16126863 Both genetic and cellular analyses indicate that auxin and the ER pathway regulate cell division and cell expansion in a largely independent but overlapping manner during elaboration of inflorescence architecture. |
| GO:0051302 regulation of cell division | IMP PMID:16007076 The ERECTA gene regulates plant transpiration efficiency in ... | KEEP AS NON CORE | Summary: erecta alters mesophyll cell proliferation. Reason: Output of ERECTA signalling; non-core. Supporting Evidence: PMID:16007076 Mechanisms include, but are not limited to, effects on stomatal density, epidermal cell expansion, mesophyll cell proliferation and cell-cell contact. |
| GO:0070370 cellular heat acclimation | IMP PMID:26280413 Overexpression of receptor-like kinase ERECTA improves therm... | KEEP AS NON CORE | Summary: er mutants are heat hypersensitive; ERECTA overexpression confers thermotolerance. Reason: Genuine but secondary physiological role. Supporting Evidence: PMID:26280413 Arabidopsis er mutants are hypersensitive to heat |
| GO:0090567 reproductive shoot system development | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA prediction of reproductive shoot system development. Reason: Consistent with ERECTA's role in inflorescence architecture; general. |
| GO:0106310 protein serine kinase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Rhea-based mapping to protein serine kinase activity. Reason: Consistent with ERECTA's Ser/Thr kinase activity. |
| GO:1904159 megasporocyte differentiation | IGI PMID:37606225 Epigenetic regulation of female germline development through... | KEEP AS NON CORE | Summary: ERECTA pathway with SWR1/SDG2 controls megasporocyte (MMC) differentiation. Reason: Reproductive developmental role; non-core. Supporting Evidence: PMID:37606225 genetically interact with the ERECTA (ER) receptor kinase signaling pathway and regulate female germline development by restricting the MMC cell fate to a single cell in the ovule primordium |
| GO:1905421 regulation of plant organ morphogenesis | IMP PMID:8624444 The Arabidopsis ERECTA gene encodes a putative receptor prot... | ACCEPT | Summary: er alleles alter the shape of organs from the shoot apical meristem. Reason: Founding evidence for ERECTA's role in organ shape; part of its principal growth-regulatory function. Supporting Evidence: PMID:8624444 Phenotypic characterization of the mutant alleles suggests a role for the ER gene in regulating the shape of organs originating from the shoot apical meristem. |
| GO:0004675 transmembrane receptor protein serine/threonine kinase activity | IDA PMID:22241782 Direct interaction of ligand-receptor pairs specifying stoma... | NEW | Summary: ERECTA directly binds EPF peptides through its LRR ectodomain and transduces the signal through its Ser/Thr kinase domain, transphosphorylating with SERK co-receptors. Reason: More specific than the existing ISS transmembrane receptor protein kinase activity and the separate Ser/Thr kinase annotations; combines direct ligand-binding evidence with kinase transphosphorylation. Supporting Evidence: PMID:22241782 Here we report the direct, robust, and saturable binding of bioactive EPF peptides to the ERECTA family. PMID:26320950 SERK and ERECTA family RLKs transphosphorylate each other. |
Loading supporting content…
Download this section (compressed HTML)Q: Which residues/phosphorylation events link EPF2-ERECTA-SERK activation to YODA, and is the BIN2/brassinosteroid input acting at the receptor or at YODA?
Q: How does ERECTA discriminate agonist (EPF2) from antagonist (stomagen) occupancy, given that both bind the same TMM-ERECTA complex but only EPF2 triggers MAPK activation?
Experiment: Phosphoproteomics of ERECTA and SERK kinase domains after MEPF2 versus stomagen treatment in seedlings, combined with kinase-dead ERECTA complementation, to define the activation-specific phosphosites.
Type: phosphoproteomics / genetic complementation
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)