The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Identity is verified. The requested protein is the Arabidopsis thaliana protein CASPL1D1 (At4g15610; UniProt Q9FE29), also called CASP-like protein 1D1/AtCASPL1D1. The locus identity, organism, and CASP-like designation agree between the supplied UniProt record and Arabidopsis primary literature; no similarly named protein from another organism was used. The supplied CASP/CASPL InterPro/Pfam assignments are consistent with literature describing the Arabidopsis CASP-like family as small, four-pass integral-membrane proteins related to the MARVEL superfamily. Arabidopsis has approximately 39 CASP/CASPL-family members. (champeyroux2019regulationofa pages 1-2, barbosa2023directedgrowthand pages 1-2)
The gene symbol is not ambiguous in this context, but gene-specific literature is limited. The best-supported primary function is nonenzymatic organization of specialized plasma-membrane/cell-wall interfaces, particularly lignified barriers induced during immunity. CASPL1D1 is not a demonstrated enzyme, channel, or transporter: no catalytic reaction, enzyme substrate specificity, transported substrate, or intrinsic transport activity has been reported. Its precise molecular mechanism remains unresolved, and detailed mechanisms established for canonical endodermal CASP1–CASP5 should be treated as family-level inference rather than CASPL1D1-specific fact. (lee2019lignin‐basedbarrierrestricts pages 6-8, barbosa2023directedgrowthand pages 12-13, barbosa2023directedgrowthand pages 1-2)
| Topic | Conclusion | Evidence type | Key quantitative observation | Confidence |
|---|---|---|---|---|
| Identity | CASPL1D1 is Arabidopsis thaliana locus At4g15610, matching the supplied UniProt accession Q9FE29 and CASP-like annotation; no different organism or similarly named protein is considered. (champeyroux2019regulationofa pages 1-2, champeyroux2019regulationofa pages 2-3) | Direct CASPL1D1 | Arabidopsis CASP/CASPL family: 39 members. (champeyroux2019regulationofa pages 1-2) | High |
| Molecular class and primary function | CASPL1D1 is best classified as a CASP-like integral membrane protein with a probable organizational/scaffold role. No catalytic reaction, enzyme substrate, transport activity, or transported substrate has been demonstrated. (barbosa2023directedgrowthand pages 1-2, champeyroux2019regulationofa pages 1-2) | Family inference | Canonical CASPs are small proteins with four transmembrane spans; applicability of their detailed mechanism to CASPL1D1 remains unproven. (barbosa2023directedgrowthand pages 1-2) | High for noncatalytic classification; moderate for scaffold inference |
| Root expression and localization | A promoter reporter was active in root tips, young tissues, and broadly across root cell types; CASPL1D1–GFP was concentrated in cortex near the root tip and continued along the root. It localized to the cortical-cell plasma membrane and was excluded from the canonical Casparian-strip domain. (champeyroux2019regulationofa pages 4-6) | Direct CASPL1D1 | The localization construct used a 1,906-bp promoter. (champeyroux2019regulationofa pages 2-3) | High |
| Root suberization | Joint disruption of CASPL1D1 and CASPL1D2 sometimes modestly enlarged the continuously suberized zone, suggesting a weak, context-dependent negative influence on suberization rather than an essential biosynthetic role. (champeyroux2019regulationofa pages 6-8) | Combined-mutant | Continuous suberization: 42% versus 36% in control conditions; 56% versus 50% after NaCl; 58% versus 58% after ABA. CASPL1D1 transcript was reduced 73% in the single line and 76% in the double mutant. (champeyroux2019regulationofa pages 6-8) | Low–moderate because the phenotype was small, inconsistent, and not assignable to CASPL1D1 alone |
| Root hydraulics and solute transport | CASPL1D1/CASPL1D2 loss did not significantly alter hydraulic conductivity, osmotic permeability, or solute flow; CASPL1D1 is therefore not established as a water or solute transporter. (champeyroux2019regulationofa pages 8-10, champeyroux2019regulationofa pages 6-8) | Combined-mutant | ABA reduced hydrostatic conductivity by 49% in the double mutant versus 53% in control; NaCl inhibition was 70% versus 52%, but the difference was not significant. (champeyroux2019regulationofa pages 8-10) | High for absence of a major measured phenotype; not proof of no subtle function |
| Aquaporin relationship | CASPL1D1 copurified in a GFP–PIP2;1 interactome, but direct CASPL1D1–PIP2;1 binding or regulation was not demonstrated. Direct interaction/function tests instead concerned CASPL1B1 and CASPL1D2, so their effects must not be transferred to CASPL1D1. (champeyroux2019regulationofa pages 1-2, champeyroux2019regulationofa pages 10-11, champeyroux2019regulationofa pages 8-10) | Direct CASPL1D1 screen plus paralog evidence | PIP2;1 increased oocyte water permeability eightfold; CASPL1B1—not CASPL1D1—added 25%. (champeyroux2019regulationofa pages 10-11) | Low for a CASPL1D1 regulatory interaction |
| Pathogen-induced lignification | CASPL1D1 knockdown reduced pathogen-induced lignification; combined CASPL1D1 knockdown and caspl4d1 mutation caused a stronger defect. Lignification persisted, indicating cooperation with CASPL4D1 and additional factors rather than exclusive control by CASPL1D1. (lee2019lignin‐basedbarrierrestricts pages 6-8) | Direct knockdown and combined-mutant | No exact CASPL1D1-specific fold change or lignin percentage was reported in the extracted evidence. (lee2019lignin‐basedbarrierrestricts pages 6-8) | Moderate–high for participation; low for its precise molecular action |
| Immune-barrier function | CASPL1D1-deficient material showed spread of hypersensitive-response cell death beyond the inoculation site and weaker restriction of avirulent Pseudomonas growth; defects were stronger with caspl4d1. The proposed role is organization of a lignified apoplastic barrier during immune responses. (lee2019lignin‐basedbarrierrestricts pages 6-8, kim2020thearabidopsisr2r3 pages 5-8) | Direct knockdown and combined-mutant | Phenotypes involved AvrRpm1- and AvrRpt2-expressing bacteria; the available excerpts provide no exact CASPL1D1-specific bacterial titres. (lee2019lignin‐basedbarrierrestricts pages 6-8) | Moderate–high for barrier participation; moderate for the structural mechanism |
| 2023 canonical-CASP model | Canonical CASP1–CASP5 organize membrane–wall adhesion, protein-exclusion zones, exocyst dynamics, and fusion of lignified microdomains. This modern scaffold model is plausible for CASPL1D1 but was not tested on CASPL1D1. (barbosa2023directedgrowthand pages 12-13, barbosa2023directedgrowthand pages 1-2) | Family inference | In the five-CASP knockout, mature lignin occupied about 50% of the wild-type area; CASP1 proximity labeling recovered 332 enriched proteins, including 32 also reduced in myb36. (barbosa2023directedgrowthand pages 11-12, barbosa2023directedgrowthand pages 2-3) | High for CASP1–5; low–moderate when extrapolated to CASPL1D1 |
Table: Evidence is separated into CASPL1D1-specific observations, combined-mutant findings, and inferences from canonical CASPs. The table highlights that CASPL1D1 is most defensibly viewed as a membrane-associated barrier organizer, not a demonstrated enzyme or transporter.
CASPL1D1 is explicitly identified in the literature as At4g15610 in A. thaliana, confirming that the retrieved studies concern the requested Q9FE29 target. The UniProt description supplied by the user—CASP-like protein 1D1, CASP/CASPL domains—is therefore concordant with the literature. (champeyroux2019regulationofa pages 1-2, champeyroux2019regulationofa pages 2-3)
Canonical Arabidopsis CASPs are small proteins with four transmembrane helices, intracellular termini, and homology to eukaryotic MARVEL-domain proteins such as animal occludins. The broader Arabidopsis family contains 39 members in five MARVEL-related subfamilies. These properties support classifying CASPL1D1 as an integral-membrane domain-organizing protein, but the detailed topology was established at family/canonical-CASP level rather than experimentally mapped for Q9FE29 itself. (barbosa2023directedgrowthand pages 12-13, barbosa2023directedgrowthand pages 1-2, barbosa2023directedgrowthand pages 11-12)
Accordingly, the most defensible molecular-function annotation is:
Probable plasma-membrane scaffold or organizer involved in coupling specialized membrane domains to localized cell-wall modification, especially immune-induced lignification.
This is substantially better supported than annotations implying catalytic or transport activity.
The strongest CASPL1D1-specific localization study used a 1,906-bp CASPL1D1 promoter and CASPL1D1–GFP fusion. Promoter-reporter activity occurred in root tips and young tissues and was broadly detectable across root cell types. The fusion protein was especially concentrated in cortical cells near the root tip and remained detectable along the root. At subcellular resolution, it localized to the cortical-cell plasma membrane. Importantly, it was excluded from the canonical endodermal Casparian-strip domain, arguing against simply assigning CASPL1D1 the same root localization as CASP1–CASP5. (champeyroux2019regulationofa pages 4-6, champeyroux2019regulationofa pages 2-3)
CASPL1D1 expression has also been reported in cells overlying lateral-root bases, a territory associated with suberization, and was strongly induced—approximately 300-fold—in plants overexpressing the suberization regulator MYB41. These observations associate it with membrane/cell-wall remodeling, although they do not prove that CASPL1D1 catalyzes suberin synthesis. (champeyroux2019regulationofa pages 6-8)
Leaf immune studies did not provide equivalent CASPL1D1-specific live-cell localization. Therefore, its exact membrane microdomain and molecular partners at infection sites remain open questions. Localization of CASPL4D1 adjacent to pathogen-induced lignin supports a family model but cannot be transferred uncritically to CASPL1D1. (lee2019lignin‐basedbarrierrestricts pages 8-10, lee2019lignin‐basedbarrierrestricts pages 6-8)
The strongest functional evidence comes from Lee et al., published December 2019 in The EMBO Journal (DOI 10.15252/embj.2019101948). CASPL1D1 transcripts accumulated after challenge with avirulent Pseudomonas syringae pv. tomato DC3000 carrying AvrRpm1. Because a suitable insertion mutant was unavailable, the researchers generated artificial-microRNA knockdown lines. CASPL1D1 knockdown substantially reduced pathogen-induced lignification, allowed hypersensitive-response cell death to spread beyond the inoculation area, and weakened restriction of AvrRpm1- and AvrRpt2-expressing bacteria. (lee2019lignin‐basedbarrierrestricts pages 6-8, lee2019lignin‐basedbarrierrestricts pages 4-6)
Combining CASPL1D1 knockdown with a caspl4d1 mutation produced still less lignin, greater spread of cell death, and stronger bacterial-growth phenotypes. Lignification was reduced rather than abolished, indicating that CASPL1D1 and CASPL4D1 cooperate nonredundantly and that other organizers also contribute. Evidence also implicated this CASPL combination in pattern-triggered responses, although the best-developed experiments concerned effector-triggered immunity. (lee2019lignin‐basedbarrierrestricts pages 6-8)
The resulting mechanistic model is that CASPL proteins help organize a Casparian-strip-like lignified barrier in the leaf apoplast. The barrier seals or partitions extracellular space, decreases bacterial motility and spread, and spatially confines hypersensitive cell death. CASPL1D1 is thus better described as part of the machinery that positions or structures lignification than as a lignin-biosynthetic enzyme. Exact CASPL1D1-specific lignin percentages and bacterial titres were not available in the extracted evidence, limiting quantitative assignment of effect size. (lee2019lignin‐basedbarrierrestricts pages 8-10, lee2019lignin‐basedbarrierrestricts pages 6-8)
CASPL1D1 participates downstream or alongside inducible phenylpropanoid/lignin production during incompatible bacterial interactions. A September 2020 study in Frontiers in Plant Science (DOI 10.3389/fpls.2020.583153) placed this barrier response in a MYB15-controlled lignification program: MYB15 activates lignin-biosynthetic genes, and MYB15-dependent lignification restricts bacterial spread and spreading hypersensitive cell death. The study used CASPL-deficient material to support the requirement for CASPL-organized lignin accumulation, but it did not establish direct MYB15 binding to the CASPL1D1 promoter or a unique CASPL1D1 biochemical mechanism. (kim2020thearabidopsisr2r3 pages 5-8, kim2020thearabidopsisr2r3 pages 2-3)
The pathway can therefore be summarized cautiously as:
pathogen perception/ETI → MYB15-dependent induction of lignin biosynthesis → CASPL1D1/CASPL4D1-dependent organization of localized lignified apoplastic structures → confinement of bacteria and cell death.
The first and last relationships are experimentally supported; the precise physical step executed by CASPL1D1 remains inferred.
Champeyroux et al., published March 2019 in Plant, Cell & Environment (DOI 10.1111/pce.13537), investigated CASPL1D1 with CASPL1D2 in roots. CASPL1D1 transcript abundance was reduced by 73% in the caspl1d1.1 line and 76% in the caspl1d1/caspl1d2 double mutant. In one experiment, continuously suberized endodermal cells increased from 36% in control to 42% in the double mutant; after NaCl, values were 50% versus 56%, whereas ABA yielded 58% in both genotypes. The effect was small and inconsistent, supporting at most a weak, context-dependent negative influence of CASPL1D1/1D2 on continuous suberization. It cannot be assigned to CASPL1D1 alone. (champeyroux2019regulationofa pages 6-8)
The mutants had no significant change in solute flow, hydrostatic hydraulic conductivity, or osmotic hydraulic conductivity. ABA reduced hydrostatic conductivity by 53% in control and 49% in the double mutant; NaCl reductions were 52% and 70%, respectively, without a significant genotype effect. Thus CASPL1D1 is not established as a water/solute transporter and does not have a major nonredundant role in whole-root hydraulic conductance under the tested conditions. (champeyroux2019regulationofa pages 8-10, champeyroux2019regulationofa pages 6-8)
CASPL1D1 was among four CASPL proteins recovered in a GFP–PIP2;1 aquaporin interactome. However, direct interaction and functional assays in the 2019 study focused on CASPL1B1 and CASPL1D2—not CASPL1D1. PIP2;1 increased Xenopus-oocyte water permeability eightfold, and CASPL1B1 added 25%; these values must not be attributed to CASPL1D1. Coexpression in root cortical plasma membranes makes a CASPL1D1–PIP2;1 relationship plausible, but direct binding, stabilization, or gating by CASPL1D1 remains unproven. (champeyroux2019regulationofa pages 4-6, champeyroux2019regulationofa pages 10-11, champeyroux2019regulationofa pages 8-10)
No 2023–2024 primary study directly resolving CASPL1D1 function was identified in the targeted searches. The major recent advance is instead a July 2023 Nature Communications study of canonical CASP1–CASP5 (DOI 10.1038/s41467-023-37265-7). It substantially refined expert understanding of what CASP-family membrane proteins do. (barbosa2023directedgrowthand pages 12-13, barbosa2023directedgrowthand pages 1-2)
In a five-CASP knockout, correctly positioned lignin microdomains still formed, showing that CASPs are not strictly required to activate or spatially initiate lignin polymerization. However, the domains failed to organize and fuse normally: walls became excessive and heterogeneous, plasma-membrane/cell-wall adhesion and protein-exclusion zones were lost, and mature lignin occupied only about 50% of the wild-type area. This shifted the canonical-CASP model from “recruiters required for lignification” toward organizers of membrane-wall microdomain growth, architecture, and fusion. (barbosa2023directedgrowthand pages 12-13, barbosa2023directedgrowthand pages 1-2, barbosa2023directedgrowthand pages 2-3)
Mechanistically, canonical CASPs appear to displace EXO70A1-marked secretory foci and exclude vesicle-tethering factors after CASP arrival, causing secretion to move along the median cell-wall zone until neighboring lignified microdomains fuse. CASP1 proximity labeling recovered 332 enriched proteins, including 32 also reduced in the myb36 mutant, and implicated RabA-family GTPases/exocyst regulation. Arabidopsis has 23 EXO70 proteins and 26 RabA GTPases, illustrating the trafficking-system complexity surrounding these domains. (barbosa2023directedgrowthand pages 12-13, barbosa2023directedgrowthand pages 11-12)
This is the best current structural analogy for CASPL1D1: it may organize an immune-induced membrane-wall platform that shapes lignin deposition and seals the apoplast. Nevertheless, CASPL1D1 was not among the canonical CASP1–CASP5 proteins tested, and its cortical localization outside the root Casparian-strip domain shows that paralogs can be spatially and functionally specialized. Confidence in transferring the exact EXO70/Rab mechanism to CASPL1D1 is therefore only low to moderate.
CASPL1D1 presently has research applications, not a validated commercial or agronomic implementation:
No evidence was found for a deployed CASPL1D1-based crop trait, diagnostic, chemical target, or biotechnology product.
The literature supports the following curated annotation:
Molecular function: probable integral-plasma-membrane scaffold/domain organizer; no demonstrated catalytic or transport activity.
Biological process: organization of pathogen-induced lignified apoplastic barriers; possible weak modulation of root endodermal suberization in conjunction with CASPL1D2.
Cellular component: plasma membrane, experimentally demonstrated in root cortical cells; exact leaf infection-site microdomain remains unresolved.
Pathway: inducible immune lignification associated with ETI and probably aspects of PTI, connected to MYB15-driven lignin biosynthesis and cooperating with CASPL4D1.
Evidence strength: moderate-to-high for participation in immune lignification and pathogen confinement; high for root cortical plasma-membrane localization; low-to-moderate for a root-suberization role; low for direct PIP2;1 regulation; currently inferential for EXO70/Rab-mediated microdomain organization.
The most important unresolved experiments are endogenous-tag localization during infection, clean null alleles with complementation, direct proximity/interactome analysis, tests of EXO70/Rab recruitment, and quantitative lignin chemistry/imaging in single and higher-order mutants. Until those are available, CASPL1D1 should not be annotated as an enzyme, transporter, direct aquaporin regulator, or canonical Casparian-strip component.
References
(champeyroux2019regulationofa pages 1-2): Chloé Champeyroux, Jorge Bellati, Marie Barberon, Valérie Rofidal, Christophe Maurel, and Véronique Santoni. Regulation of a plant aquaporin by a casparian strip membrane domain protein-like. Plant, cell & environment, 42 6:1788-1801, Mar 2019. URL: https://doi.org/10.1111/pce.13537, doi:10.1111/pce.13537. This article has 21 citations.
(barbosa2023directedgrowthand pages 1-2): Inês Catarina Ramos Barbosa, D. De Bellis, Isabelle Flückiger, E. Bellani, Mathieu Grangé-Guerment, Kian Hématy, and N. Geldner. Directed growth and fusion of membrane-wall microdomains requires casp-mediated inhibition and displacement of secretory foci. Nature Communications, Jul 2023. URL: https://doi.org/10.1038/s41467-023-37265-7, doi:10.1038/s41467-023-37265-7. This article has 36 citations and is from a highest quality peer-reviewed journal.
(lee2019lignin‐basedbarrierrestricts pages 6-8): Myoung‐Hoon Lee, Hwi Seong Jeon, Seu Ha Kim, Joo Hee Chung, Daniele Roppolo, Hye‐Jung Lee, Hong Joo Cho, Yuki Tobimatsu, John Ralph, and Ohkmae K Park. Lignin‐based barrier restricts pathogens to the infection site and confers resistance in plants. The EMBO Journal, Dec 2019. URL: https://doi.org/10.15252/embj.2019101948, doi:10.15252/embj.2019101948. This article has 493 citations.
(barbosa2023directedgrowthand pages 12-13): Inês Catarina Ramos Barbosa, D. De Bellis, Isabelle Flückiger, E. Bellani, Mathieu Grangé-Guerment, Kian Hématy, and N. Geldner. Directed growth and fusion of membrane-wall microdomains requires casp-mediated inhibition and displacement of secretory foci. Nature Communications, Jul 2023. URL: https://doi.org/10.1038/s41467-023-37265-7, doi:10.1038/s41467-023-37265-7. This article has 36 citations and is from a highest quality peer-reviewed journal.
(champeyroux2019regulationofa pages 2-3): Chloé Champeyroux, Jorge Bellati, Marie Barberon, Valérie Rofidal, Christophe Maurel, and Véronique Santoni. Regulation of a plant aquaporin by a casparian strip membrane domain protein-like. Plant, cell & environment, 42 6:1788-1801, Mar 2019. URL: https://doi.org/10.1111/pce.13537, doi:10.1111/pce.13537. This article has 21 citations.
(champeyroux2019regulationofa pages 4-6): Chloé Champeyroux, Jorge Bellati, Marie Barberon, Valérie Rofidal, Christophe Maurel, and Véronique Santoni. Regulation of a plant aquaporin by a casparian strip membrane domain protein-like. Plant, cell & environment, 42 6:1788-1801, Mar 2019. URL: https://doi.org/10.1111/pce.13537, doi:10.1111/pce.13537. This article has 21 citations.
(champeyroux2019regulationofa pages 6-8): Chloé Champeyroux, Jorge Bellati, Marie Barberon, Valérie Rofidal, Christophe Maurel, and Véronique Santoni. Regulation of a plant aquaporin by a casparian strip membrane domain protein-like. Plant, cell & environment, 42 6:1788-1801, Mar 2019. URL: https://doi.org/10.1111/pce.13537, doi:10.1111/pce.13537. This article has 21 citations.
(champeyroux2019regulationofa pages 8-10): Chloé Champeyroux, Jorge Bellati, Marie Barberon, Valérie Rofidal, Christophe Maurel, and Véronique Santoni. Regulation of a plant aquaporin by a casparian strip membrane domain protein-like. Plant, cell & environment, 42 6:1788-1801, Mar 2019. URL: https://doi.org/10.1111/pce.13537, doi:10.1111/pce.13537. This article has 21 citations.
(champeyroux2019regulationofa pages 10-11): Chloé Champeyroux, Jorge Bellati, Marie Barberon, Valérie Rofidal, Christophe Maurel, and Véronique Santoni. Regulation of a plant aquaporin by a casparian strip membrane domain protein-like. Plant, cell & environment, 42 6:1788-1801, Mar 2019. URL: https://doi.org/10.1111/pce.13537, doi:10.1111/pce.13537. This article has 21 citations.
(kim2020thearabidopsisr2r3 pages 5-8): Seu Ha Kim, Pui Ying Lam, Myoung-Hoon Lee, Hwi Seong Jeon, Yuki Tobimatsu, and Ohkmae K. Park. The arabidopsis r2r3 myb transcription factor myb15 is a key regulator of lignin biosynthesis in effector-triggered immunity. Frontiers in Plant Science, Sep 2020. URL: https://doi.org/10.3389/fpls.2020.583153, doi:10.3389/fpls.2020.583153. This article has 160 citations.
(barbosa2023directedgrowthand pages 11-12): Inês Catarina Ramos Barbosa, D. De Bellis, Isabelle Flückiger, E. Bellani, Mathieu Grangé-Guerment, Kian Hématy, and N. Geldner. Directed growth and fusion of membrane-wall microdomains requires casp-mediated inhibition and displacement of secretory foci. Nature Communications, Jul 2023. URL: https://doi.org/10.1038/s41467-023-37265-7, doi:10.1038/s41467-023-37265-7. This article has 36 citations and is from a highest quality peer-reviewed journal.
(barbosa2023directedgrowthand pages 2-3): Inês Catarina Ramos Barbosa, D. De Bellis, Isabelle Flückiger, E. Bellani, Mathieu Grangé-Guerment, Kian Hématy, and N. Geldner. Directed growth and fusion of membrane-wall microdomains requires casp-mediated inhibition and displacement of secretory foci. Nature Communications, Jul 2023. URL: https://doi.org/10.1038/s41467-023-37265-7, doi:10.1038/s41467-023-37265-7. This article has 36 citations and is from a highest quality peer-reviewed journal.
(lee2019lignin‐basedbarrierrestricts pages 8-10): Myoung‐Hoon Lee, Hwi Seong Jeon, Seu Ha Kim, Joo Hee Chung, Daniele Roppolo, Hye‐Jung Lee, Hong Joo Cho, Yuki Tobimatsu, John Ralph, and Ohkmae K Park. Lignin‐based barrier restricts pathogens to the infection site and confers resistance in plants. The EMBO Journal, Dec 2019. URL: https://doi.org/10.15252/embj.2019101948, doi:10.15252/embj.2019101948. This article has 493 citations.
(lee2019lignin‐basedbarrierrestricts pages 4-6): Myoung‐Hoon Lee, Hwi Seong Jeon, Seu Ha Kim, Joo Hee Chung, Daniele Roppolo, Hye‐Jung Lee, Hong Joo Cho, Yuki Tobimatsu, John Ralph, and Ohkmae K Park. Lignin‐based barrier restricts pathogens to the infection site and confers resistance in plants. The EMBO Journal, Dec 2019. URL: https://doi.org/10.15252/embj.2019101948, doi:10.15252/embj.2019101948. This article has 493 citations.
(kim2020thearabidopsisr2r3 pages 2-3): Seu Ha Kim, Pui Ying Lam, Myoung-Hoon Lee, Hwi Seong Jeon, Yuki Tobimatsu, and Ohkmae K. Park. The arabidopsis r2r3 myb transcription factor myb15 is a key regulator of lignin biosynthesis in effector-triggered immunity. Frontiers in Plant Science, Sep 2020. URL: https://doi.org/10.3389/fpls.2020.583153, doi:10.3389/fpls.2020.583153. This article has 160 citations.