ABCG36 (PENETRATION3/PEN3, PLEIOTROPIC DRUG RESISTANCE8/PDR8) is a full-size pleiotropic drug resistance-type ABC transporter of the ABCG subfamily that acts as an ATP-dependent exporter of small molecules across the plasma membrane. In leaves it is uniformly distributed in the epidermal plasma membrane and, after perception of fungal or bacterial molecular patterns, is focally recruited to sites of attempted pathogen penetration where it accumulates in papillae; there it exports tryptophan-derived defense metabolites, including the phytoalexin camalexin and products of the PEN2 myrosinase-dependent indole glucosinolate pathway, contributing to pre-invasive nonhost resistance against powdery mildews and other fungi, and to defense against oomycetes and bacteria. In roots it occupies the outer lateral plasma-membrane domain of epidermal cells, where, redundantly with ABCG37, it exports the auxin precursor indole-3-butyric acid (but not IAA), influencing auxin homeostasis and root and cotyledon growth. It also mediates cadmium extrusion and contributes to heavy-metal tolerance. Its substrate preference is regulated by phosphorylation: the receptor kinase QSK1 represses IBA export in favor of camalexin export, and the transporter interacts with calmodulin Ca2+ sensors. PEN3 cycles between the plasma membrane and the trans-Golgi network.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000325 plant-type vacuole | HDA PMID:17151019 A proteomics dissection of Arabidopsis thaliana vacuoles iso... | MARK AS OVER ANNOTATED | Summary: Plant-type vacuole from vacuolar proteomics. Reason: Targeted studies localize PEN3 to the plasma membrane and not the vacuole; proteomic detection likely reflects contamination or trafficking. Supporting Evidence: PMID:19095898 PEN3 localizes to the plasma membrane, not the vacuole PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0002229 defense response to oomycetes | IMP PMID:24889055 Role of the penetration-resistance genes PEN1, PEN2 and PEN3... | KEEP AS NON CORE | Summary: Defense response to oomycetes; pen3 mutants are compromised in resistance to Phytophthora infestans and avirulent Hyaloperonospora arabidopsidis. Reason: Genuine contribution to defense against oomycetes through the same extracellular export mechanism, but secondary to antifungal penetration resistance. Supporting Evidence: PMID:24889055 resistance to avirulent isolates of the oomycete Hyaloperonospora arabidopsidis was strongly compromised |
| GO:0002229 defense response to oomycetes | IMP PMID:26023163 Mutant Allele-Specific Uncoupling of PENETRATION3 Functions ... | KEEP AS NON CORE | Summary: Defense response to oomycetes; pen3 mutants are compromised in resistance to Phytophthora infestans and avirulent Hyaloperonospora arabidopsidis. Reason: Genuine contribution to defense against oomycetes through the same extracellular export mechanism, but secondary to antifungal penetration resistance. Supporting Evidence: PMID:26023163 This metabolic pathway directs the intracellular biosynthesis and activation of tryptophan-derived indole glucosinolates for subsequent PEN3-mediated efflux across the plasma membrane at pathogen contact sites. PMID:16473969 pen3 mutants were compromised in resistance to the necrotroph Plectosphaerella cucumerina and to two additional inappropriate biotrophs, pea powdery mildew (Erysiphe pisi) and potato late blight (Phytophthora infestans) |
| GO:0002237 response to molecule of bacterial origin | IDA PMID:28434950 An Arabidopsis Lipid Flippase Is Required for Timely Recruit... | KEEP AS NON CORE | Summary: Response to molecule of bacterial origin; PEN3 is focally recruited after flg22 perception, and flg22-induced callose requires PEN3. Reason: Accurate description of PEN3 relocalization/requirement downstream of bacterial PAMP perception; a response-type annotation, not the core transport function. Supporting Evidence: PMID:28434950 recruited to sites of pathogen detection where it accumulates within papillae |
| GO:0002237 response to molecule of bacterial origin | IEP PMID:23815470 Induction and suppression of PEN3 focal accumulation during ... | KEEP AS NON CORE | Summary: Response to molecule of bacterial origin; PEN3 is focally recruited after flg22 perception, and flg22-induced callose requires PEN3. Reason: Accurate description of PEN3 relocalization/requirement downstream of bacterial PAMP perception; a response-type annotation, not the core transport function. Supporting Evidence: PMID:23815470 P. syringae pv. tomato DC3000 infection or treatment with a flagellin-derived peptide, flg22, induced strong focal accumulation of PEN3-green fluorescent protein |
| GO:0002237 response to molecule of bacterial origin | IEP PMID:23836668 Perception of conserved pathogen elicitors at the plasma mem... | KEEP AS NON CORE | Summary: Response to molecule of bacterial origin; PEN3 is focally recruited after flg22 perception, and flg22-induced callose requires PEN3. Reason: Accurate description of PEN3 relocalization/requirement downstream of bacterial PAMP perception; a response-type annotation, not the core transport function. Supporting Evidence: PMID:23836668 We report that recruitment of PEN3 to sites of pathogen detection is triggered by perception of pathogen-associated molecular patterns, such as flagellin and chitin. |
| GO:0002237 response to molecule of bacterial origin | IMP PMID:24889055 Role of the penetration-resistance genes PEN1, PEN2 and PEN3... | KEEP AS NON CORE | Summary: Response to molecule of bacterial origin; PEN3 is focally recruited after flg22 perception, and flg22-induced callose requires PEN3. Reason: Accurate description of PEN3 relocalization/requirement downstream of bacterial PAMP perception; a response-type annotation, not the core transport function. Supporting Evidence: PMID:24889055 We found that loss of function mutations in any of the three PEN genes cause decreased hypersensitive cell death triggered by recognition of effectors from oomycete and bacterial pathogens in Arabidopsis. |
| GO:0002237 response to molecule of bacterial origin | IMP PMID:26023163 Mutant Allele-Specific Uncoupling of PENETRATION3 Functions ... | KEEP AS NON CORE | Summary: Response to molecule of bacterial origin; PEN3 is focally recruited after flg22 perception, and flg22-induced callose requires PEN3. Reason: Accurate description of PEN3 relocalization/requirement downstream of bacterial PAMP perception; a response-type annotation, not the core transport function. Supporting Evidence: PMID:26023163 The specific mutation in pen3-5 uncouples PEN3 functions in IBA-stimulated root growth modulation, callose deposition induced with a conserved peptide epitope of bacterial flagellin (flg22), and pathogen-inducible salicylic acid accumulation from PEN3 activity in extracellular defense |
| GO:0002238 response to molecule of fungal origin | IDA PMID:28434950 An Arabidopsis Lipid Flippase Is Required for Timely Recruit... | KEEP AS NON CORE | Summary: Response to molecule of fungal origin; chitin perception via PRRs triggers PEN3 recruitment to pathogen contact sites. Reason: Supported by relocalization data in response to chitin; descriptive response annotation, non-core. Supporting Evidence: PMID:28434950 recruited to sites of pathogen detection where it accumulates within papillae |
| GO:0002238 response to molecule of fungal origin | IEP PMID:23836668 Perception of conserved pathogen elicitors at the plasma mem... | KEEP AS NON CORE | Summary: Response to molecule of fungal origin; chitin perception via PRRs triggers PEN3 recruitment to pathogen contact sites. Reason: Supported by relocalization data in response to chitin; descriptive response annotation, non-core. Supporting Evidence: PMID:23836668 We report that recruitment of PEN3 to sites of pathogen detection is triggered by perception of pathogen-associated molecular patterns, such as flagellin and chitin. PMID:23836668 PEN3 recruitment requires the corresponding pattern recognition receptors but does not require the BAK1 coreceptor. |
| GO:0002239 response to oomycetes | IEP PMID:24889055 Role of the penetration-resistance genes PEN1, PEN2 and PEN3... | KEEP AS NON CORE | Summary: Response to oomycetes (expression/response data in Johansson et al.). Reason: PEN3 participates in responses to oomycete pathogens (HR and resistance to avirulent H. arabidopsidis); response-level annotation, non-core. Supporting Evidence: PMID:24889055 We found that loss of function mutations in any of the three PEN genes cause decreased hypersensitive cell death triggered by recognition of effectors from oomycete and bacterial pathogens in Arabidopsis. PMID:24889055 resistance to avirulent isolates of the oomycete Hyaloperonospora arabidopsidis was strongly compromised |
| GO:0002240 response to molecule of oomycetes origin | IMP PMID:24889055 Role of the penetration-resistance genes PEN1, PEN2 and PEN3... | KEEP AS NON CORE | Summary: Response to molecule of oomycetes origin; pen mutants show reduced HR triggered by recognized oomycete effectors. Reason: Supported by reduced effector-triggered cell death in pen3 mutants; non-core consequence of PEN3 metabolite export. Supporting Evidence: PMID:24889055 We found that loss of function mutations in any of the three PEN genes cause decreased hypersensitive cell death triggered by recognition of effectors from oomycete and bacterial pathogens in Arabidopsis. |
| GO:0003729 mRNA binding | IDA PMID:32344669 Discovering the RNA-Binding Proteome of Plant Leaves with an... | MARK AS OVER ANNOTATED | Summary: mRNA binding from leaf RNA interactome capture. Reason: A plasma-membrane ABC transporter with no RNA-binding domain; detection in high-throughput RIC is not evidence of a biologically meaningful mRNA-binding function. Supporting Evidence: PMID:32344669 a large proportion of leaf RBPs lack known RNA-binding domains |
| GO:0005515 protein binding | IPI PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | MODIFY | Summary: Protein binding from Ca2+-dependent interaction with calmodulins CaM3/CaM7, CaM-like proteins and Ca2+-binding proteins (CBL4, KIC) via the N-terminal cytoplasmic domain. Reason: Protein binding is uninformative. The interactions are with calmodulin and calmodulin-like Ca2+ sensors (CaM7 confirmed in vivo by BiFC); calmodulin binding is the informative term. Proposed replacements: calmodulin binding Supporting Evidence: PMID:26315018 we confirmed PEN3-CaM interaction in vitro and in vivo by PEN3 pull-down with CaM Sepharose, CaM overlay assay and bimolecular fluorescence complementation PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005515 protein binding | IPI PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | MODIFY | Summary: Protein binding from Ca2+-dependent interaction with calmodulins CaM3/CaM7, CaM-like proteins and Ca2+-binding proteins (CBL4, KIC) via the N-terminal cytoplasmic domain. Reason: Protein binding is uninformative. The interactions are with calmodulin and calmodulin-like Ca2+ sensors (CaM7 confirmed in vivo by BiFC); calmodulin binding is the informative term. Proposed replacements: calmodulin binding Supporting Evidence: PMID:26315018 we confirmed PEN3-CaM interaction in vitro and in vivo by PEN3 pull-down with CaM Sepharose, CaM overlay assay and bimolecular fluorescence complementation PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005515 protein binding | IPI PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | MODIFY | Summary: Protein binding from Ca2+-dependent interaction with calmodulins CaM3/CaM7, CaM-like proteins and Ca2+-binding proteins (CBL4, KIC) via the N-terminal cytoplasmic domain. Reason: Protein binding is uninformative. The interactions are with calmodulin and calmodulin-like Ca2+ sensors (CaM7 confirmed in vivo by BiFC); calmodulin binding is the informative term. Proposed replacements: calmodulin binding Supporting Evidence: PMID:26315018 we confirmed PEN3-CaM interaction in vitro and in vivo by PEN3 pull-down with CaM Sepharose, CaM overlay assay and bimolecular fluorescence complementation PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005515 protein binding | IPI PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | MODIFY | Summary: Protein binding from Ca2+-dependent interaction with calmodulins CaM3/CaM7, CaM-like proteins and Ca2+-binding proteins (CBL4, KIC) via the N-terminal cytoplasmic domain. Reason: Protein binding is uninformative. The interactions are with calmodulin and calmodulin-like Ca2+ sensors (CaM7 confirmed in vivo by BiFC); calmodulin binding is the informative term. Proposed replacements: calmodulin binding Supporting Evidence: PMID:26315018 we confirmed PEN3-CaM interaction in vitro and in vivo by PEN3 pull-down with CaM Sepharose, CaM overlay assay and bimolecular fluorescence complementation PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005515 protein binding | IPI PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | MODIFY | Summary: Protein binding from Ca2+-dependent interaction with calmodulins CaM3/CaM7, CaM-like proteins and Ca2+-binding proteins (CBL4, KIC) via the N-terminal cytoplasmic domain. Reason: Protein binding is uninformative. The interactions are with calmodulin and calmodulin-like Ca2+ sensors (CaM7 confirmed in vivo by BiFC); calmodulin binding is the informative term. Proposed replacements: calmodulin binding Supporting Evidence: PMID:26315018 we confirmed PEN3-CaM interaction in vitro and in vivo by PEN3 pull-down with CaM Sepharose, CaM overlay assay and bimolecular fluorescence complementation PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005515 protein binding | IPI PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | MODIFY | Summary: Protein binding from Ca2+-dependent interaction with calmodulins CaM3/CaM7, CaM-like proteins and Ca2+-binding proteins (CBL4, KIC) via the N-terminal cytoplasmic domain. Reason: Protein binding is uninformative. The interactions are with calmodulin and calmodulin-like Ca2+ sensors (CaM7 confirmed in vivo by BiFC); calmodulin binding is the informative term. Proposed replacements: calmodulin binding Supporting Evidence: PMID:26315018 we confirmed PEN3-CaM interaction in vitro and in vivo by PEN3 pull-down with CaM Sepharose, CaM overlay assay and bimolecular fluorescence complementation PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005515 protein binding | IPI PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | MODIFY | Summary: Protein binding from Ca2+-dependent interaction with calmodulins CaM3/CaM7, CaM-like proteins and Ca2+-binding proteins (CBL4, KIC) via the N-terminal cytoplasmic domain. Reason: Protein binding is uninformative. The interactions are with calmodulin and calmodulin-like Ca2+ sensors (CaM7 confirmed in vivo by BiFC); calmodulin binding is the informative term. Proposed replacements: calmodulin binding Supporting Evidence: PMID:26315018 we confirmed PEN3-CaM interaction in vitro and in vivo by PEN3 pull-down with CaM Sepharose, CaM overlay assay and bimolecular fluorescence complementation PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005515 protein binding | IPI PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | MODIFY | Summary: Protein binding from Ca2+-dependent interaction with calmodulins CaM3/CaM7, CaM-like proteins and Ca2+-binding proteins (CBL4, KIC) via the N-terminal cytoplasmic domain. Reason: Protein binding is uninformative. The interactions are with calmodulin and calmodulin-like Ca2+ sensors (CaM7 confirmed in vivo by BiFC); calmodulin binding is the informative term. Proposed replacements: calmodulin binding Supporting Evidence: PMID:26315018 we confirmed PEN3-CaM interaction in vitro and in vivo by PEN3 pull-down with CaM Sepharose, CaM overlay assay and bimolecular fluorescence complementation PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005515 protein binding | IPI PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | MODIFY | Summary: Protein binding from Ca2+-dependent interaction with calmodulins CaM3/CaM7, CaM-like proteins and Ca2+-binding proteins (CBL4, KIC) via the N-terminal cytoplasmic domain. Reason: Protein binding is uninformative. The interactions are with calmodulin and calmodulin-like Ca2+ sensors (CaM7 confirmed in vivo by BiFC); calmodulin binding is the informative term. Proposed replacements: calmodulin binding Supporting Evidence: PMID:26315018 we confirmed PEN3-CaM interaction in vitro and in vivo by PEN3 pull-down with CaM Sepharose, CaM overlay assay and bimolecular fluorescence complementation PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding from InterPro ABC transporter domain. Reason: ABCG36 has two nucleotide-binding domains and catalyses ATP-dependent export. Supporting Evidence: PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| GO:0005739 mitochondrion | HDA PMID:15276431 The hydrophobic proteome of mitochondrial membranes from Ara... | MARK AS OVER ANNOTATED | Summary: Mitochondrion from mitochondrial membrane proteomics. Reason: Likely membrane-fraction contamination; targeted studies place ABCG36 at the plasma membrane. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0005739 mitochondrion | ISM GO_REF:0000122 | MARK AS OVER ANNOTATED | Summary: Mitochondrion predicted by sequence-based targeting analysis. Reason: Computational prediction for a protein with extensive experimental localization to the plasma membrane and no evidence for mitochondrial targeting, so the prediction adds no support for a mitochondrial pool. The same mitochondrion claim also carries an HDA membrane-proteomics row (PMID:15276431) that is MARK_AS_OVER_ANNOTATED, and no experimental NOT mitochondrion exists, so rows sharing the term take that one action rather than REMOVE (ARATH organelle audit tie-break, projects/ARATH/organelle-audit.md). Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. PMID:16415066 Subcellular fractionation and immunochemical analysis showed that AtPDR8 was localized in the plasma membrane. |
| GO:0005783 endoplasmic reticulum | IDA PMID:29085068 Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficki... | MARK AS OVER ANNOTATED | Summary: Endoplasmic reticulum (membrane); PEN3 transits the ER and is ER-arrested in eap3 mutants. Reason: ER residence is a biosynthetic transit step common to all plasma-membrane proteins and is prominent only in the eap3 mutant; it is not a functional location of ABCG36. Supporting Evidence: PMID:29085068 specifically mediates PEN3 exit from the endoplasmic reticulum and confers resistance to a root-penetrating fungus |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:29085068 Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficki... | MARK AS OVER ANNOTATED | Summary: Endoplasmic reticulum (membrane); PEN3 transits the ER and is ER-arrested in eap3 mutants. Reason: ER residence is a biosynthetic transit step common to all plasma-membrane proteins and is prominent only in the eap3 mutant; it is not a functional location of ABCG36. Supporting Evidence: PMID:29085068 specifically mediates PEN3 exit from the endoplasmic reticulum and confers resistance to a root-penetrating fungus |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | MARK AS OVER ANNOTATED | Summary: Endoplasmic reticulum (membrane); PEN3 transits the ER and is ER-arrested in eap3 mutants. Reason: ER residence is a biosynthetic transit step common to all plasma-membrane proteins and is prominent only in the eap3 mutant; it is not a functional location of ABCG36. Supporting Evidence: PMID:29085068 specifically mediates PEN3 exit from the endoplasmic reticulum and confers resistance to a root-penetrating fungus |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Golgi apparatus mapped from UniProt subcellular location (trans-Golgi network membrane). Reason: Consistent with TGN cycling of PEN3; trafficking location, non-core. Supporting Evidence: PMID:28434950 We provide evidence that PEN3 undergoes continuous endocytic cycling from the PM to the trans-Golgi network (TGN). |
| GO:0005802 trans-Golgi network | IDA PMID:27803190 A Framework for Lateral Membrane Trafficking and Polar Tethe... | KEEP AS NON CORE | Summary: Trans-Golgi network; PEN3 continuously cycles between the plasma membrane and the TGN. Reason: Supported by direct imaging; a trafficking compartment rather than the site of transport function. Supporting Evidence: PMID:27803190 from the trans-Golgi network (TGN) to the plasma membrane in the root epidermis of Arabidopsis |
| GO:0005802 trans-Golgi network | IDA PMID:28434950 An Arabidopsis Lipid Flippase Is Required for Timely Recruit... | KEEP AS NON CORE | Summary: Trans-Golgi network; PEN3 continuously cycles between the plasma membrane and the TGN. Reason: Supported by direct imaging; a trafficking compartment rather than the site of transport function. Supporting Evidence: PMID:28434950 We provide evidence that PEN3 undergoes continuous endocytic cycling from the PM to the trans-Golgi network (TGN). |
| GO:0005886 plasma membrane | EXP PMID:16415066 Loss of AtPDR8, a plasma membrane ABC transporter of Arabido... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:16415066 Subcellular fractionation and immunochemical analysis showed that AtPDR8 was localized in the plasma membrane. |
| GO:0005886 plasma membrane | EXP PMID:28910579 Phosphorylation is required for the pathogen defense functio... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:28910579 The Arabidopsis PEN3 ABC transporter accumulates at sites of pathogen detection PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0005886 plasma membrane | HDA PMID:14506206 Large-scale analysis of in vivo phosphorylated membrane prot... | ACCEPT | Summary: Plasma membrane detected in a large-scale proteomics / phosphoproteomics study; consistent with extensive targeted localization data. Reason: High-throughput detection agrees with GFP-fusion and immunolocalization studies placing ABCG36 at the plasma membrane, where it exports its substrates. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. PMID:16415066 Subcellular fractionation and immunochemical analysis showed that AtPDR8 was localized in the plasma membrane. |
| GO:0005886 plasma membrane | HDA PMID:16618929 Mapping the Arabidopsis organelle proteome. | ACCEPT | Summary: Plasma membrane detected in a large-scale proteomics / phosphoproteomics study; consistent with extensive targeted localization data. Reason: High-throughput detection agrees with GFP-fusion and immunolocalization studies placing ABCG36 at the plasma membrane, where it exports its substrates. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. PMID:16415066 Subcellular fractionation and immunochemical analysis showed that AtPDR8 was localized in the plasma membrane. |
| GO:0005886 plasma membrane | HDA PMID:17644812 A high content in lipid-modified peripheral proteins and int... | ACCEPT | Summary: Plasma membrane detected in a large-scale proteomics / phosphoproteomics study; consistent with extensive targeted localization data. Reason: High-throughput detection agrees with GFP-fusion and immunolocalization studies placing ABCG36 at the plasma membrane, where it exports its substrates. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. PMID:16415066 Subcellular fractionation and immunochemical analysis showed that AtPDR8 was localized in the plasma membrane. |
| GO:0005886 plasma membrane | HDA PMID:22923678 Putative glycosyltransferases and other plant Golgi apparatu... | ACCEPT | Summary: Plasma membrane detected in a large-scale proteomics / phosphoproteomics study; consistent with extensive targeted localization data. Reason: High-throughput detection agrees with GFP-fusion and immunolocalization studies placing ABCG36 at the plasma membrane, where it exports its substrates. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. PMID:16415066 Subcellular fractionation and immunochemical analysis showed that AtPDR8 was localized in the plasma membrane. |
| GO:0005886 plasma membrane | IDA PMID:16473969 Arabidopsis PEN3/PDR8, an ATP binding cassette transporter, ... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0005886 plasma membrane | IDA PMID:17355438 The ABC transporter AtPDR8 is a cadmium extrusion pump confe... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:17355438 The GFP-AtPDR8 protein was targeted to the plasma membrane |
| GO:0005886 plasma membrane | IDA PMID:19648296 The Arabidopsis PLEIOTROPIC DRUG RESISTANCE8/ABCG36 ATP bind... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:19648296 a plasma membrane-localized ATP binding cassette transporter |
| GO:0005886 plasma membrane | IDA PMID:20451385 Trafficking to the outer polar domain defines the root-soil ... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:20451385 we analyze the mechanism of polar delivery to the root-soil interface of the proteins BOR4, ABCG37, and PEN3 PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0005886 plasma membrane | IDA PMID:20498067 Arabidopsis PIS1 encodes the ABCG37 transporter of auxinic c... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:20498067 ABCG37 and its homolog ABCG36 act redundantly at outermost root plasma membranes and, unlike established IAA transporters from the PIN and ABCB families, transport IBA out of the cells. |
| GO:0005886 plasma membrane | IDA PMID:23836668 Perception of conserved pathogen elicitors at the plasma mem... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:23836668 PEN3 resides in the plasma membrane |
| GO:0005886 plasma membrane | IDA PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:26315018 In Arabidopsis, NHR requires membrane-localized ATP-binding cassette (ABC) transporter PENETRATION (PEN) 3. PMID:26315018 We demonstrated co-localization of PEN3 and CaM7 |
| GO:0005886 plasma membrane | IDA PMID:27803190 A Framework for Lateral Membrane Trafficking and Polar Tethe... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:27803190 the EXOCYST84b (EXO84b) tethering factor mediates PEN3 outer-membrane polarity PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0005886 plasma membrane | IDA PMID:29085068 Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficki... | ACCEPT | Summary: ABCG36/PEN3 is an integral plasma-membrane PDR-type ABC transporter; plasma membrane is its site of action. This study localized it there (GFP fusion, fractionation or immunolocalization). Reason: Direct experimental localization; the plasma membrane (including the outer lateral domain of root epidermis and focal penetration sites) is the core location of ABCG36 activity. Supporting Evidence: PMID:29085068 The epidermal outer plasma membrane domain harbours the PENETRATION3 (PEN3)/ABCG36/PDR8 ATP-binding cassette transporter |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Plasma membrane location mapped from UniProt subcellular location keywords. Reason: Correct; ABCG36 is a plasma-membrane transporter, as shown repeatedly by experimental localization. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. PMID:16415066 Subcellular fractionation and immunochemical analysis showed that AtPDR8 was localized in the plasma membrane. |
| GO:0009408 response to heat | IEP PMID:31358650 Transcriptional Profiling Reveals a Time-of-Day-Specific Rol... | MARK AS OVER ANNOTATED | Summary: Response to heat based on RNA-seq of heat-shock-induced transcripts. Reason: High-throughput transcript change only; no evidence that ABCG36 performs any step of the heat response. Supporting Evidence: PMID:31358650 RNA sequencing was performed to detect genes whose expression is rapidly altered by HS in Arabidopsis |
| GO:0009414 response to water deprivation | IMP PMID:20088904 Overexpression of AtABCG36 improves drought and salt stress ... | KEEP AS NON CORE | Summary: Response to water deprivation; knockout lines are more drought-sensitive and overexpressors more tolerant. Reason: Phenotypic evidence for a contribution to drought tolerance, mechanism unclear (possibly reduced sodium content); non-core. Supporting Evidence: PMID:20088904 T-DNA insertional knockout lines were more sensitive to drought stress than wild-type |
| GO:0009507 chloroplast | HDA PMID:18431481 Sorting signals, N-terminal modifications and abundance of t... | REMOVE | Summary: Chloroplast from chloroplast proteomics. Reason: Directly contradicted by targeted GFP localization to the plasma membrane and by the experimental NOT chloroplast annotation from the same localization work; the proteomic hit is most likely contamination. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0009507 chloroplast | IDA NOT PMID:16473969 Arabidopsis PEN3/PDR8, an ATP binding cassette transporter, ... | ACCEPT | Summary: NOT located in chloroplast; GFP-tagged PEN3 localized to the plasma membrane. Reason: The negative annotation is consistent with all targeted localization data. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0009617 response to bacterium | IEP PMID:23815470 Induction and suppression of PEN3 focal accumulation during ... | KEEP AS NON CORE | Summary: Response to bacterium; PEN3 accumulates focally upon Pseudomonas infection and its expression/function responds to bacterial challenge. Reason: Descriptive response annotation; correct but non-core. Supporting Evidence: PMID:23815470 P. syringae pv. tomato DC3000 infection or treatment with a flagellin-derived peptide, flg22, induced strong focal accumulation of PEN3-green fluorescent protein |
| GO:0009617 response to bacterium | IEP PMID:24889055 Role of the penetration-resistance genes PEN1, PEN2 and PEN3... | KEEP AS NON CORE | Summary: Response to bacterium; PEN3 accumulates focally upon Pseudomonas infection and its expression/function responds to bacterial challenge. Reason: Descriptive response annotation; correct but non-core. Supporting Evidence: PMID:24889055 We found that loss of function mutations in any of the three PEN genes cause decreased hypersensitive cell death triggered by recognition of effectors from oomycete and bacterial pathogens in Arabidopsis. |
| GO:0009620 response to fungus | IEP PMID:20605856 Entry mode-dependent function of an indole glucosinolate pat... | KEEP AS NON CORE | Summary: Response to fungus; PEN3 expression is induced by fungal challenge (e.g. Colletotrichum gloeosporioides). Reason: Expression-based response annotation; correct but the more informative defense response to fungus term captures the core role. Supporting Evidence: PMID:20605856 Expression of PEN2 , PEN3 , CYP79B2 , and CYP81F2 was each found to be pathogen inducible as early as 9 hpi |
| GO:0009620 response to fungus | IEP PMID:24889055 Role of the penetration-resistance genes PEN1, PEN2 and PEN3... | KEEP AS NON CORE | Summary: Response to fungus; PEN3 expression is induced by fungal challenge (e.g. Colletotrichum gloeosporioides). Reason: Expression-based response annotation; correct but the more informative defense response to fungus term captures the core role. Supporting Evidence: PMID:24889055 the double and triple mutants demonstrated varying degrees of run-away cell death in response to Bgh |
| GO:0009626 plant-type hypersensitive response | IMP PMID:24889055 Role of the penetration-resistance genes PEN1, PEN2 and PEN3... | KEEP AS NON CORE | Summary: Plant-type hypersensitive response; pen3 mutations reduce effector-triggered HR cell death and Kobae et al. describe AtPDR8 as controlling the extent of cell death. Reason: PEN3 modulates HR via export of indole glucosinolate breakdown products; a genuine but secondary role relative to penetration resistance. Supporting Evidence: PMID:24889055 We found that loss of function mutations in any of the three PEN genes cause decreased hypersensitive cell death triggered by recognition of effectors from oomycete and bacterial pathogens in Arabidopsis. PMID:16415066 Our results indicate that AtPDR8 is a key factor controlling the extent of cell death in the defense response |
| GO:0009627 systemic acquired resistance | IMP PMID:16473969 Arabidopsis PEN3/PDR8, an ATP binding cassette transporter, ... | MARK AS OVER ANNOTATED | Summary: Systemic acquired resistance, based on SA-pathway hyperinduction and SA-dependent resistance to an adapted powdery mildew in pen3. Reason: The pen3 SA phenotypes are interpreted as secondary consequences of intracellular toxin accumulation; ABCG36 is not a component of systemic acquired resistance signaling. Supporting Evidence: PMID:16473969 intracellular accumulation of these toxins in pen3 may secondarily activate the salicylic acid pathway |
| GO:0009651 response to salt stress | IMP PMID:20088904 Overexpression of AtABCG36 improves drought and salt stress ... | KEEP AS NON CORE | Summary: Response to salt stress; overexpressing plants are more salt-tolerant. Reason: Phenotypic association; non-core abiotic stress role. Supporting Evidence: PMID:20088904 AtABCG36-overexpressing plants were more resistant to drought and salt stress PMID:20088904 AtABCG36 overexpressing plants were lower in sodium content than the wild-type |
| GO:0009733 response to auxin | IMP PMID:26023163 Mutant Allele-Specific Uncoupling of PENETRATION3 Functions ... | KEEP AS NON CORE | Summary: Response to auxin; pen3-5 uncouples IBA-stimulated root growth modulation. Reason: The phenotype reflects altered IBA efflux; ABCG36 transports the auxin precursor rather than mediating the auxin response itself. Kept as non-core. Supporting Evidence: PMID:26023163 The specific mutation in pen3-5 uncouples PEN3 functions in IBA-stimulated root growth modulation, callose deposition induced with a conserved peptide epitope of bacterial flagellin (flg22), and pathogen-inducible salicylic acid accumulation from PEN3 activity in extracellular defense PMID:19648296 We found that pdr8 mutants display defects in efflux of the auxin precursor IBA and developmental defects in root hair and cotyledon expansion |
| GO:0009804 coumarin metabolic process | IMP PMID:28623273 Arabidopsis Transporter ABCG37/PDR9 contributes primarily hi... | MARK AS OVER ANNOTATED | Summary: Coumarin metabolic process from root-exudate metabolomics of pdr8/pdr9. Reason: Coumarin exudation is mainly ABCG37-dependent; any ABCG36 contribution would be export, not coumarin metabolism. Supporting Evidence: PMID:28623273 Esculetin exhibited a similar pattern in roots, but in exudates a change could only be detected for pdr8-1. PMID:28623273 This suggests partial compensations of ABCG36 function in pdr8-1 by ABCG37 |
| GO:0009926 auxin polar transport | IMP PMID:20498067 Arabidopsis PIS1 encodes the ABCG37 transporter of auxinic c... | KEEP AS NON CORE | Summary: Auxin polar transport; ABCG36 and ABCG37 export IBA at the outer polar domain of root epidermal cells. Reason: ABCG36 exports IBA laterally from polarly localized outer membrane domains; this contributes to directional auxin(-precursor) movement but differs from canonical PIN/ABCB IAA polar transport. Non-core. Supporting Evidence: PMID:20498067 ABCG37 and its homolog ABCG36 act redundantly at outermost root plasma membranes and, unlike established IAA transporters from the PIN and ABCB families, transport IBA out of the cells. PMID:20451385 we analyze the mechanism of polar delivery to the root-soil interface of the proteins BOR4, ABCG37, and PEN3 |
| GO:0009941 chloroplast envelope | HDA PMID:12938931 Proteomic study of the Arabidopsis thaliana chloroplastic en... | REMOVE | Summary: Chloroplast envelope from envelope proteomics. Reason: Plasma-membrane protein; envelope detection likely contamination. ARATH organelle consistency: this review ACCEPTs the experimental NOT chloroplast annotation (PMID:16473969), which entails NOT for every chloroplast sub-compartment, and REMOVEs the positive HDA chloroplast row; the positive chloroplast envelope row (part_of chloroplast) is removed for the same reason rather than kept as over-annotated. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0010200 response to chitin | IEP PMID:23836668 Perception of conserved pathogen elicitors at the plasma mem... | KEEP AS NON CORE | Summary: Response to chitin; chitin perception triggers PEN3 focal recruitment. Reason: Supported relocalization response; non-core. Supporting Evidence: PMID:23836668 We report that recruitment of PEN3 to sites of pathogen detection is triggered by perception of pathogen-associated molecular patterns, such as flagellin and chitin. |
| GO:0010315 auxin export across the plasma membrane | IEA GO_REF:0000108 | ACCEPT | Summary: Auxin export across the plasma membrane, inferred from the auxin efflux transporter activity annotation. Reason: Correct logical inference; ABCG36 exports IBA across the plasma membrane of root epidermal cells. Supporting Evidence: PMID:20498067 ABCG37 and its homolog ABCG36 act redundantly at outermost root plasma membranes and, unlike established IAA transporters from the PIN and ABCB families, transport IBA out of the cells. PMID:19648296 We found that pdr8 mutants display defects in efflux of the auxin precursor IBA and developmental defects in root hair and cotyledon expansion |
| GO:0010329 auxin efflux transmembrane transporter activity | IDA PMID:20498067 Arabidopsis PIS1 encodes the ABCG37 transporter of auxinic c... | ACCEPT | Summary: Auxin efflux transmembrane transporter activity; ABCG36 (with ABCG37) exports the auxin precursor IBA, but not IAA, out of root cells. Reason: Directly supported by IBA efflux assays; IBA is a naturally occurring auxin. Wild-type ABCG36 does not export IAA, which should be noted, but the term is appropriate. Supporting Evidence: PMID:20498067 ABCG37 and its homolog ABCG36 act redundantly at outermost root plasma membranes and, unlike established IAA transporters from the PIN and ABCB families, transport IBA out of the cells. PMID:19648296 We found that pdr8 mutants display defects in efflux of the auxin precursor IBA and developmental defects in root hair and cotyledon expansion file:ARATH/ABCG36/ABCG36-deep-research-falcon.md Wild-type ABCG36 did not increase IAA export or show IAA-stimulated ATPase activity. |
| GO:0010928 regulation of auxin mediated signaling pathway | IMP PMID:19648296 The Arabidopsis PLEIOTROPIC DRUG RESISTANCE8/ABCG36 ATP bind... | KEEP AS NON CORE | Summary: Regulation of auxin-mediated signaling pathway; PDR8-promoted IBA efflux limits IBA-derived IAA. Reason: Reasonable regulatory consequence of IBA efflux on auxin homeostasis; non-core. Supporting Evidence: PMID:19648296 Our results are consistent with the possibility that limiting accumulation of the IAA precursor IBA via PDR8-promoted efflux contributes to auxin homeostasis. |
| GO:0015086 cadmium ion transmembrane transporter activity | IDA PMID:17355438 The ABC transporter AtPDR8 is a cadmium extrusion pump confe... | KEEP AS NON CORE | Summary: Cadmium ion transmembrane transporter activity; 109Cd flux assays in protoplasts show ABCG36-dependent Cd extrusion. Reason: Supported by flux assays, though the transported species (free Cd2+ vs Cd conjugate) is unresolved; a non-core activity of this multispecific exporter. Supporting Evidence: PMID:17355438 these data strongly support a role for AtPDR8 as an efflux pump of Cd(2+) or Cd conjugates at the plasma membrane of Arabidopsis cells file:ARATH/ABCG36/ABCG36-deep-research-falcon.md Supports cadmium extrusion and tolerance, but the molecular substrate should be annotated conservatively as Cd²⁺ and/or a Cd conjugate. |
| GO:0015562 efflux transmembrane transporter activity | IMP PMID:19648296 The Arabidopsis PLEIOTROPIC DRUG RESISTANCE8/ABCG36 ATP bind... | ACCEPT | Summary: Efflux transmembrane transporter activity; ABCG36 exports multiple substrates (IBA, indolic defense metabolites, camalexin) out of the cell. Reason: Correct and appropriately general for this multispecific PDR exporter; the general efflux term usefully covers substrates (e.g. glucosinolate-pathway products, root exudates) for which no specific transporter term exists. Supporting Evidence: PMID:19648296 We found that pdr8 mutants display defects in efflux of the auxin precursor IBA and developmental defects in root hair and cotyledon expansion |
| GO:0015562 efflux transmembrane transporter activity | IMP PMID:20498067 Arabidopsis PIS1 encodes the ABCG37 transporter of auxinic c... | ACCEPT | Summary: Efflux transmembrane transporter activity; ABCG36 exports multiple substrates (IBA, indolic defense metabolites, camalexin) out of the cell. Reason: Correct and appropriately general for this multispecific PDR exporter; the general efflux term usefully covers substrates (e.g. glucosinolate-pathway products, root exudates) for which no specific transporter term exists. Supporting Evidence: PMID:20498067 ABCG37 and its homolog ABCG36 act redundantly at outermost root plasma membranes and, unlike established IAA transporters from the PIN and ABCB families, transport IBA out of the cells. |
| GO:0015562 efflux transmembrane transporter activity | IMP PMID:26023163 Mutant Allele-Specific Uncoupling of PENETRATION3 Functions ... | ACCEPT | Summary: Efflux transmembrane transporter activity; ABCG36 exports multiple substrates (IBA, indolic defense metabolites, camalexin) out of the cell. Reason: Correct and appropriately general for this multispecific PDR exporter; the general efflux term usefully covers substrates (e.g. glucosinolate-pathway products, root exudates) for which no specific transporter term exists. Supporting Evidence: PMID:26023163 This metabolic pathway directs the intracellular biosynthesis and activation of tryptophan-derived indole glucosinolates for subsequent PEN3-mediated efflux across the plasma membrane at pathogen contact sites. |
| GO:0015562 efflux transmembrane transporter activity | IMP PMID:28623273 Arabidopsis Transporter ABCG37/PDR9 contributes primarily hi... | ACCEPT | Summary: Efflux transmembrane transporter activity; ABCG36 exports multiple substrates (IBA, indolic defense metabolites, camalexin) out of the cell. Reason: Correct and appropriately general for this multispecific PDR exporter; the general efflux term usefully covers substrates (e.g. glucosinolate-pathway products, root exudates) for which no specific transporter term exists. Supporting Evidence: PMID:28623273 Irrespective of the unknown role of thymidine exudation in Arabidopsis, its decreased level in pdr8-1 provides evidence that thymidine exudation is an active process and not merely a consequence of root cell death PMID:28623273 This suggests partial compensations of ABCG36 function in pdr8-1 by ABCG37 |
| GO:0015691 cadmium ion transport | IMP PMID:17355438 The ABC transporter AtPDR8 is a cadmium extrusion pump confe... | KEEP AS NON CORE | Summary: Cadmium ion transport; ABCG36 mediates Cd extrusion and confers Cd/Pb tolerance. Reason: Supported; non-core relative to defense metabolite and IBA export. Supporting Evidence: PMID:17355438 these data strongly support a role for AtPDR8 as an efflux pump of Cd(2+) or Cd conjugates at the plasma membrane of Arabidopsis cells |
| GO:0016020 membrane | IEA GO_REF:0000002 | ACCEPT | Summary: Membrane from InterPro. Reason: Correct but general; plasma membrane is the specific location. Supporting Evidence: PMID:16473969 PEN3/PDR8 tagged with green fluorescent protein localized to the plasma membrane in uninfected cells. In infected leaves, the protein concentrated at infection sites. |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | ACCEPT | Summary: ATP hydrolysis activity from InterPro. Reason: Consistent with ATP-dependent transport by the NBDs. Supporting Evidence: PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| GO:0031348 negative regulation of defense response | IMP PMID:16732289 Conserved requirement for a plant host cell protein in powde... | MARK AS OVER ANNOTATED | Summary: Negative regulation of defense response from mlo epistasis/pen3 phenotypes (chlorosis, deregulated defense). Reason: ABCG36 is a positive effector of defense (exporter of antimicrobials); enhanced defense/cell-death phenotypes in pen3 are secondary effects, not evidence that ABCG36 acts as a negative regulator. Abstract-only access; curator's interpretation not contradicted outright, so not removed. Supporting Evidence: PMID:16732289 but requires a syntaxin, glycosyl hydrolase and ABC transporter PMID:16473969 intracellular accumulation of these toxins in pen3 may secondarily activate the salicylic acid pathway |
| GO:0042344 indole glucosinolate catabolic process | IMP PMID:19095898 Glucosinolate metabolites required for an Arabidopsis innate... | MARK AS OVER ANNOTATED | Summary: Indole glucosinolate catabolic process; PEN3 is required for flg22-induced accumulation of 4-methoxy-I3G hydrolysis products. Reason: The hydrolysis of 4-methoxy-indol-3-ylmethyl glucosinolate is catalysed by the PEN2 myrosinase (with PCS1); ABCG36 exports the products. Requirement for the pathway output is necessity, not participation in the catabolic chemistry. Supporting Evidence: PMID:19095898 Two genes, PEN2 and PEN3, are also necessary for resistance to pathogens and are required for both callose deposition and glucosinolate activation PMID:19095898 the PEN2, PCS1, and PEN3-mediated hydrolysis of 4-methoxy-I3G PMID:26023163 This metabolic pathway directs the intracellular biosynthesis and activation of tryptophan-derived indole glucosinolates for subsequent PEN3-mediated efflux across the plasma membrane at pathogen contact sites. |
| GO:0042742 defense response to bacterium | IDA PMID:28434950 An Arabidopsis Lipid Flippase Is Required for Timely Recruit... | KEEP AS NON CORE | Summary: Defense response to bacterium; pen3 mutants show reduced PTI-associated outputs and compromised resistance to Pseudomonas syringae. Reason: Supported, and plausibly via the same export of indolic defense metabolites, but bacterial defense is secondary to the well-established antifungal penetration resistance role; Johansson et al. found that loss of HR in pen double mutants did not affect bacterial growth restriction. Supporting Evidence: PMID:28434950 recruited to sites of pathogen detection where it accumulates within papillae |
| GO:0042742 defense response to bacterium | IMP PMID:19095898 Glucosinolate metabolites required for an Arabidopsis innate... | KEEP AS NON CORE | Summary: Defense response to bacterium; pen3 mutants show reduced PTI-associated outputs and compromised resistance to Pseudomonas syringae. Reason: Supported, and plausibly via the same export of indolic defense metabolites, but bacterial defense is secondary to the well-established antifungal penetration resistance role; Johansson et al. found that loss of HR in pen double mutants did not affect bacterial growth restriction. Supporting Evidence: PMID:19095898 Two genes, PEN2 and PEN3, are also necessary for resistance to pathogens and are required for both callose deposition and glucosinolate activation |
| GO:0042742 defense response to bacterium | IMP PMID:23815470 Induction and suppression of PEN3 focal accumulation during ... | KEEP AS NON CORE | Summary: Defense response to bacterium; pen3 mutants show reduced PTI-associated outputs and compromised resistance to Pseudomonas syringae. Reason: Supported, and plausibly via the same export of indolic defense metabolites, but bacterial defense is secondary to the well-established antifungal penetration resistance role; Johansson et al. found that loss of HR in pen double mutants did not affect bacterial growth restriction. Supporting Evidence: PMID:23815470 we show that the pen3 mutant is compromised in resistance to the bacterial pathogen Pseudomonas syringae pv. tomato DC3000 |
| GO:0042742 defense response to bacterium | IMP PMID:24889055 Role of the penetration-resistance genes PEN1, PEN2 and PEN3... | KEEP AS NON CORE | Summary: Defense response to bacterium; pen3 mutants show reduced PTI-associated outputs and compromised resistance to Pseudomonas syringae. Reason: Supported, and plausibly via the same export of indolic defense metabolites, but bacterial defense is secondary to the well-established antifungal penetration resistance role; Johansson et al. found that loss of HR in pen double mutants did not affect bacterial growth restriction. Supporting Evidence: PMID:24889055 We found that loss of function mutations in any of the three PEN genes cause decreased hypersensitive cell death triggered by recognition of effectors from oomycete and bacterial pathogens in Arabidopsis. PMID:24889055 the loss of the HR in pen double mutants did not affect the plants' ability to restrict bacterial growth |
| GO:0042742 defense response to bacterium | IMP PMID:26023163 Mutant Allele-Specific Uncoupling of PENETRATION3 Functions ... | KEEP AS NON CORE | Summary: Defense response to bacterium; pen3 mutants show reduced PTI-associated outputs and compromised resistance to Pseudomonas syringae. Reason: Supported, and plausibly via the same export of indolic defense metabolites, but bacterial defense is secondary to the well-established antifungal penetration resistance role; Johansson et al. found that loss of HR in pen double mutants did not affect bacterial growth restriction. Supporting Evidence: PMID:26023163 The specific mutation in pen3-5 uncouples PEN3 functions in IBA-stimulated root growth modulation, callose deposition induced with a conserved peptide epitope of bacterial flagellin (flg22), and pathogen-inducible salicylic acid accumulation from PEN3 activity in extracellular defense |
| GO:0046104 thymidine metabolic process | IMP PMID:28623273 Arabidopsis Transporter ABCG37/PDR9 contributes primarily hi... | MARK AS OVER ANNOTATED | Summary: Thymidine metabolic process from reduced thymidine root exudation in pdr8-1. Reason: The phenotype concerns exudation (export) of thymidine, not its metabolism; the metabolic process term is not supported. Supporting Evidence: PMID:28623273 Irrespective of the unknown role of thymidine exudation in Arabidopsis, its decreased level in pdr8-1 provides evidence that thymidine exudation is an active process and not merely a consequence of root cell death |
| GO:0048364 root development | IMP PMID:20498067 Arabidopsis PIS1 encodes the ABCG37 transporter of auxinic c... | MARK AS OVER ANNOTATED | Summary: Root development inferred from IBA-related root phenotypes of abcg36/abcg37 mutants. Reason: Broad developmental term reflecting indirect effects of altered IBA efflux. Supporting Evidence: PMID:20498067 ABCG37 and its homolog ABCG36 act redundantly at outermost root plasma membranes and, unlike established IAA transporters from the PIN and ABCB families, transport IBA out of the cells. |
| GO:0048825 cotyledon development | IMP PMID:19648296 The Arabidopsis PLEIOTROPIC DRUG RESISTANCE8/ABCG36 ATP bind... | MARK AS OVER ANNOTATED | Summary: Cotyledon development from faster cotyledon expansion in pdr8. Reason: Developmental phenotype is an indirect consequence of increased IBA-derived IAA; ABCG36 performs no step of cotyledon development. Supporting Evidence: PMID:19648296 We found that pdr8 mutants display defects in efflux of the auxin precursor IBA and developmental defects in root hair and cotyledon expansion |
| GO:0050832 defense response to fungus | IDA PMID:28434950 An Arabidopsis Lipid Flippase Is Required for Timely Recruit... | ACCEPT | Summary: Defense response to fungus; ABCG36/PEN3 is required for nonhost penetration resistance to fungi (powdery mildews, Colletotrichum, Phakopsora, Plectosphaerella, Fusarium). Reason: ABCG36 does part of the work of pre-invasive defense: it exports antimicrobial indolic metabolites (camalexin, PEN2-pathway indole glucosinolate products) across the plasma membrane at fungal contact sites. Loss-of-function compromises resistance to multiple nonadapted fungi. Retained as the core biological process. Supporting Evidence: PMID:28434950 recruited to sites of pathogen detection where it accumulates within papillae PMID:28434950 timely exit of these proteins from the TGN is critical for effective pre-invasive immune responses against powdery mildews PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| GO:0050832 defense response to fungus | IDA PMID:29085068 Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficki... | ACCEPT | Summary: Defense response to fungus; ABCG36/PEN3 is required for nonhost penetration resistance to fungi (powdery mildews, Colletotrichum, Phakopsora, Plectosphaerella, Fusarium). Reason: ABCG36 does part of the work of pre-invasive defense: it exports antimicrobial indolic metabolites (camalexin, PEN2-pathway indole glucosinolate products) across the plasma membrane at fungal contact sites. Loss-of-function compromises resistance to multiple nonadapted fungi. Retained as the core biological process. Supporting Evidence: PMID:29085068 specifically mediates PEN3 exit from the endoplasmic reticulum and confers resistance to a root-penetrating fungus PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| GO:0050832 defense response to fungus | IMP PMID:16473969 Arabidopsis PEN3/PDR8, an ATP binding cassette transporter, ... | ACCEPT | Summary: Defense response to fungus; ABCG36/PEN3 is required for nonhost penetration resistance to fungi (powdery mildews, Colletotrichum, Phakopsora, Plectosphaerella, Fusarium). Reason: ABCG36 does part of the work of pre-invasive defense: it exports antimicrobial indolic metabolites (camalexin, PEN2-pathway indole glucosinolate products) across the plasma membrane at fungal contact sites. Loss-of-function compromises resistance to multiple nonadapted fungi. Retained as the core biological process. Supporting Evidence: PMID:16473969 pen3 mutants were compromised in resistance to the necrotroph Plectosphaerella cucumerina and to two additional inappropriate biotrophs, pea powdery mildew (Erysiphe pisi) and potato late blight (Phytophthora infestans) PMID:16473969 PEN3/PDR8 may be involved in exporting toxic materials to attempted invasion sites PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| GO:0050832 defense response to fungus | IMP PMID:20605856 Entry mode-dependent function of an indole glucosinolate pat... | ACCEPT | Summary: Defense response to fungus; ABCG36/PEN3 is required for nonhost penetration resistance to fungi (powdery mildews, Colletotrichum, Phakopsora, Plectosphaerella, Fusarium). Reason: ABCG36 does part of the work of pre-invasive defense: it exports antimicrobial indolic metabolites (camalexin, PEN2-pathway indole glucosinolate products) across the plasma membrane at fungal contact sites. Loss-of-function compromises resistance to multiple nonadapted fungi. Retained as the core biological process. Supporting Evidence: PMID:20605856 We thus determined the entry rate of Cg on pen3 plants, and it was indeed intermediate PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| GO:0050832 defense response to fungus | IMP PMID:26023163 Mutant Allele-Specific Uncoupling of PENETRATION3 Functions ... | ACCEPT | Summary: Defense response to fungus; ABCG36/PEN3 is required for nonhost penetration resistance to fungi (powdery mildews, Colletotrichum, Phakopsora, Plectosphaerella, Fusarium). Reason: ABCG36 does part of the work of pre-invasive defense: it exports antimicrobial indolic metabolites (camalexin, PEN2-pathway indole glucosinolate products) across the plasma membrane at fungal contact sites. Loss-of-function compromises resistance to multiple nonadapted fungi. Retained as the core biological process. Supporting Evidence: PMID:26023163 This metabolic pathway directs the intracellular biosynthesis and activation of tryptophan-derived indole glucosinolates for subsequent PEN3-mediated efflux across the plasma membrane at pathogen contact sites. PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| GO:0050832 defense response to fungus | IMP PMID:26315018 ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin t... | ACCEPT | Summary: Defense response to fungus; ABCG36/PEN3 is required for nonhost penetration resistance to fungi (powdery mildews, Colletotrichum, Phakopsora, Plectosphaerella, Fusarium). Reason: ABCG36 does part of the work of pre-invasive defense: it exports antimicrobial indolic metabolites (camalexin, PEN2-pathway indole glucosinolate products) across the plasma membrane at fungal contact sites. Loss-of-function compromises resistance to multiple nonadapted fungi. Retained as the core biological process. Supporting Evidence: PMID:26315018 NHR to the nonadapted fungal pathogens Phakopsora pachyrhizi and Blumeria graminis f.sp. hordei is compromised in the Arabidopsis cam7 and pen3 cam7 mutants PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| GO:0050832 defense response to fungus | IMP PMID:28910579 Phosphorylation is required for the pathogen defense functio... | ACCEPT | Summary: Defense response to fungus; ABCG36/PEN3 is required for nonhost penetration resistance to fungi (powdery mildews, Colletotrichum, Phakopsora, Plectosphaerella, Fusarium). Reason: ABCG36 does part of the work of pre-invasive defense: it exports antimicrobial indolic metabolites (camalexin, PEN2-pathway indole glucosinolate products) across the plasma membrane at fungal contact sites. Loss-of-function compromises resistance to multiple nonadapted fungi. Retained as the core biological process. Supporting Evidence: PMID:28910579 We report that PEN3 phosphorylation is critical for its function in defense, but dispensable for recruitment to powdery mildew penetration sites. PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| 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: Defense response by callose deposition in cell wall; pen3 mutants are impaired in flg22-induced callose. Reason: PEN3-exported indolic metabolites are required for callose deposition; PEN3 contributes upstream of callose synthase. Retained as non-core. Supporting Evidence: PMID:19095898 Two genes, PEN2 and PEN3, are also necessary for resistance to pathogens and are required for both callose deposition and glucosinolate activation |
| GO:0055078 sodium ion homeostasis | IMP PMID:20088904 Overexpression of AtABCG36 improves drought and salt stress ... | MARK AS OVER ANNOTATED | Summary: Sodium ion homeostasis inferred from lower sodium content in overexpressing plants. Reason: No evidence that ABCG36 transports sodium; reduced Na content in overexpressors is an indirect whole-plant phenotype. Supporting Evidence: PMID:20088904 AtABCG36 overexpressing plants were lower in sodium content than the wild-type |
| GO:0055085 transmembrane transport | IMP PMID:19648296 The Arabidopsis PLEIOTROPIC DRUG RESISTANCE8/ABCG36 ATP bind... | ACCEPT | Summary: Transmembrane transport; ABCG36 exports substrates (IBA, root exudate components) across the plasma membrane. Reason: Correct, general description of ABCG36 activity; more specific transport terms are also annotated. Supporting Evidence: PMID:19648296 We found that pdr8 mutants display defects in efflux of the auxin precursor IBA and developmental defects in root hair and cotyledon expansion |
| GO:0055085 transmembrane transport | IMP PMID:28623273 Arabidopsis Transporter ABCG37/PDR9 contributes primarily hi... | ACCEPT | Summary: Transmembrane transport; ABCG36 exports substrates (IBA, root exudate components) across the plasma membrane. Reason: Correct, general description of ABCG36 activity; more specific transport terms are also annotated. Supporting Evidence: PMID:28623273 Irrespective of the unknown role of thymidine exudation in Arabidopsis, its decreased level in pdr8-1 provides evidence that thymidine exudation is an active process and not merely a consequence of root cell death |
| GO:0070574 cadmium ion transmembrane transport | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: Cadmium ion transmembrane transport inferred from the cadmium transporter activity annotation. Reason: Consistent logical inference; non-core. Supporting Evidence: PMID:17355438 these data strongly support a role for AtPDR8 as an efflux pump of Cd(2+) or Cd conjugates at the plasma membrane of Arabidopsis cells |
| GO:0071366 cellular response to indolebutyric acid stimulus | IMP PMID:19648296 The Arabidopsis PLEIOTROPIC DRUG RESISTANCE8/ABCG36 ATP bind... | KEEP AS NON CORE | Summary: Cellular response to indolebutyric acid stimulus; pdr8/abcg36 mutants are hypersensitive to IBA. Reason: Hypersensitivity results from reduced IBA efflux; the direct function is IBA export, captured by the auxin efflux transporter terms. Supporting Evidence: PMID:19648296 We identified an Arabidopsis thaliana mutant that specifically restores IBA, but not IAA, responsiveness to auxin signaling mutants. |
| GO:0071366 cellular response to indolebutyric acid stimulus | IMP PMID:20498067 Arabidopsis PIS1 encodes the ABCG37 transporter of auxinic c... | KEEP AS NON CORE | Summary: Cellular response to indolebutyric acid stimulus; pdr8/abcg36 mutants are hypersensitive to IBA. Reason: Hypersensitivity results from reduced IBA efflux; the direct function is IBA export, captured by the auxin efflux transporter terms. Supporting Evidence: PMID:20498067 transports a range of synthetic auxinic compounds as well as the endogenous auxin precursor indole-3-butyric acid (IBA), but not free IAA |
| GO:0080147 root hair cell development | IMP PMID:19648296 The Arabidopsis PLEIOTROPIC DRUG RESISTANCE8/ABCG36 ATP bind... | MARK AS OVER ANNOTATED | Summary: Root hair cell development from longer root hairs in pdr8. Reason: Root hair phenotype requires IBA-to-IAA conversion and is an indirect auxin effect, not participation of ABCG36 in root hair development. Supporting Evidence: PMID:19648296 suggesting that conversion of IBA to IAA is required for the lengthened root hairs found in pdr8 |
| GO:0140352 export from cell | IMP PMID:16877699 A gain-of-function mutation in the Arabidopsis pleiotropic d... | ACCEPT | Summary: Export from cell, attributed to a study of the paralog PDR9/ABCG37 that mentions atpdr8 only as background. Reason: The full text of this reference does not appear to assay ABCG36 directly, so the reference is weak support; however export from cell is well established for ABCG36 (IBA, camalexin, indolic defense metabolites), so the annotation itself is correct. Supporting Evidence: PMID:16877699 An additional connection between PDR-type transporters and defense response is provided by recent studies of atpdr8 mutants, which exhibit increased cell death associated with the hypersensitive response following pathogen infection PMID:19648296 We found that pdr8 mutants display defects in efflux of the auxin precursor IBA and developmental defects in root hair and cotyledon expansion PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane |
| GO:0140352 export from cell | IMP PMID:19648296 The Arabidopsis PLEIOTROPIC DRUG RESISTANCE8/ABCG36 ATP bind... | ACCEPT | Summary: Export from cell; ABCG36 exports IBA and other metabolites (root exudates) into the extracellular space. Reason: Correct process-level description of ABCG36 export activity. Supporting Evidence: PMID:19648296 We found that pdr8 mutants display defects in efflux of the auxin precursor IBA and developmental defects in root hair and cotyledon expansion |
| GO:0140352 export from cell | IMP PMID:28623273 Arabidopsis Transporter ABCG37/PDR9 contributes primarily hi... | ACCEPT | Summary: Export from cell; ABCG36 exports IBA and other metabolites (root exudates) into the extracellular space. Reason: Correct process-level description of ABCG36 export activity. Supporting Evidence: PMID:28623273 Irrespective of the unknown role of thymidine exudation in Arabidopsis, its decreased level in pdr8-1 provides evidence that thymidine exudation is an active process and not merely a consequence of root cell death |
| GO:0140359 ABC-type transporter activity | IEA GO_REF:0000002 | ACCEPT | Summary: ABC-type transporter activity from InterPro. Reason: Correct general MF for this full-size PDR-type ABCG transporter. Supporting Evidence: PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane PMID:19648296 We found that pdr8 mutants display defects in efflux of the auxin precursor IBA and developmental defects in root hair and cotyledon expansion |
| GO:0140426 pathogen-associated molecular pattern receptor signaling pathway | IDA PMID:23836668 Perception of conserved pathogen elicitors at the plasma mem... | MARK AS OVER ANNOTATED | Summary: Pathogen-associated molecular pattern receptor signaling pathway; PRR-dependent recruitment of PEN3 to pathogen contact sites. Reason: PEN3 is a downstream cargo whose relocalization requires PRRs; it is not a signaling component of the PRR pathway. Better captured by response to molecule of bacterial/fungal origin. Supporting Evidence: PMID:23836668 We report that recruitment of PEN3 to sites of pathogen detection is triggered by perception of pathogen-associated molecular patterns, such as flagellin and chitin. PMID:23836668 PEN3 recruitment requires the corresponding pattern recognition receptors but does not require the BAK1 coreceptor. |
| GO:0160080 ABC-type indole transporter activity | IDA PMID:37146609 An LRR receptor kinase controls ABC transporter substrate pr... | ACCEPT | Summary: ABC-type indole transporter activity; ATP-dependent export of the indole phytoalexin camalexin by ABCG36. Reason: Best available MF term for ATP-dependent export of indolic defense compounds. Note the term definition names indole itself; wild-type ABCG36 transports indole derivatives (camalexin, IBA, 4MeOI3M) and indole transport was reported for an engineered L704Y variant. Supporting Evidence: PMID:37146609 we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane PMID:37146609 Phosphorylation of ABCG36 by QSK1 unilaterally represses IBA export, allowing camalexin export by ABCG36 conferring pathogen resistance. file:ARATH/ABCG36/ABCG36-deep-research-falcon.md Engineered L704Y acquired IAA and indole transport activity. |
| GO:1990748 cellular detoxification | IMP PMID:20498067 Arabidopsis PIS1 encodes the ABCG37 transporter of auxinic c... | KEEP AS NON CORE | Summary: Cellular detoxification; ABCG36/ABCG37 export synthetic auxinic herbicides (e.g. 2,4-DB). Reason: Export of xenobiotic auxinic compounds is a genuine PDR transporter activity; non-core. Supporting Evidence: PMID:20498067 transports a range of synthetic auxinic compounds as well as the endogenous auxin precursor indole-3-butyric acid (IBA), but not free IAA PMID:20498067 ABCG37 and its homolog ABCG36 act redundantly at outermost root plasma membranes and, unlike established IAA transporters from the PIN and ABCB families, transport IBA out of the cells. |
| GO:2000023 regulation of lateral root development | IMP PMID:19648296 The Arabidopsis PLEIOTROPIC DRUG RESISTANCE8/ABCG36 ATP bind... | KEEP AS NON CORE | Summary: Regulation of lateral root development; pdr8 alleles produce more lateral roots. Reason: Indirect regulation via IBA homeostasis; non-core. Supporting Evidence: PMID:19648296 Additionally, the pdr8 alleles all displayed modestly increased lateral root production in the absence of exogenous hormone |
| GO:2000071 regulation of defense response by callose deposition | IMP PMID:23815470 Induction and suppression of PEN3 focal accumulation during ... | KEEP AS NON CORE | Summary: Regulation of defense response by callose deposition (Pseudomonas/flg22 callose phenotypes). Reason: Consistent with PEN3 being required for PAMP-induced callose; non-core. Supporting Evidence: PMID:23815470 we show that the pen3 mutant is compromised in resistance to the bacterial pathogen Pseudomonas syringae pv. tomato DC3000 PMID:19095898 Two genes, PEN2 and PEN3, are also necessary for resistance to pathogens and are required for both callose deposition and glucosinolate activation |
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Download this section (compressed HTML)Q: GO:0160080 'ABC-type indole transporter activity' is defined with indole itself as substrate, but wild-type ABCG36 exports indole derivatives (camalexin, IBA, 4-methoxyindol-3-ylmethanol). Should GO broaden the definition to indole-containing compounds, or create camalexin / indole glucosinolate-product exporter terms?
Q: Which chemical species does ABCG36 actually translocate in cadmium tolerance (free Cd2+ or a glutathione/phytochelatin conjugate), and is cadmium ion transmembrane transporter activity the right MF?
Q: Is there a single molecular substrate of PEN3 in nonhost resistance to powdery mildew (4MeOI3M, 4MeOI3Cys or camalexin), and how is substrate choice regulated by PAMP-induced phosphorylation and calmodulin binding?
Experiment: Vesicular or proteoliposome transport assays with purified ABCG36 to test direct transport of candidate PEN2-pathway products (4MeOI3M, 4MeOI3Cys) and Cd-glutathione conjugates, with kinetic constants.
Experiment: Phospho-mimic/phospho-dead ABCG36 variants expressed in abcg36 backgrounds, combined with leaf-surface metabolomics after Blumeria inoculation, to link specific phosphosites to substrate export at penetration sites.
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