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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

Research Report: Functional Annotation of Arabidopsis thaliana CASPL1D2 (At3g06390; UniProt Q9SQU2)

0. Target verification (critical identity check)

The literature summarized here explicitly matches the UniProt target Q9SQU2 as CASP-like protein 1D2 (CASPL1D2) from Arabidopsis thaliana, gene/locus At3g06390 and a member of the CASP/CASPL (DUF588/PF04535; MARVEL-related 4TM) family. This avoids symbol ambiguity and ensures that evidence refers to the intended Arabidopsis protein rather than similarly named genes from other species. (champeyroux2019regulationofa pages 1-2, xue2024comparativeanalysisof pages 2-4, barbosa2023directedgrowthand pages 1-2)

1. Key concepts and definitions (current understanding)

1.1 Casparian strip and the Casparian strip membrane domain (CSD)

The Casparian strip (CS) is an aligned, lignin-impregnated cell-wall band in root endodermal cells that forms an extracellular (apoplastic) diffusion barrier. The corresponding specialized plasma-membrane region is the Casparian strip membrane domain (CSD). (barbosa2023directedgrowthand pages 1-2)

The CSD is a polar plasma-membrane domain with functional properties of a membrane diffusion barrier, limiting diffusion of endogenous membrane proteins and lipophilic dyes across the domain boundary. (jaillais2024guidelinesfornaming pages 6-8)

1.2 CASP vs CASPL proteins

CASPs (CASP1–CASP5) are described as small four-transmembrane-span proteins that form a highly stable transmembrane platform localized to the CSD; they are homologous to animal occludins, show strong endodermis-specific expression, and form microdomains that fuse into a continuous band aligned with lignification. (barbosa2023directedgrowthand pages 1-2, barbosa2023directedgrowthand pages 2-3)

Plant plasma membrane organization is increasingly framed as nested scales—nanodomains embedded in larger polar domains. In the endodermis, CASP proteins first appear in small nanodomains that coalesce into a larger polar domain forming the continuous Casparian strip belt. (jaillais2024guidelinesfornaming pages 4-6, jaillais2024guidelinesfornaming pages 8-13)

CASP-LIKE (CASPL) proteins are members of the broader CASP/CASPL family (often defined by DUF588/PF04535, and frequently associated with MARVEL-like 4TM architecture), but are not necessarily core CSD scaffolds. Arabidopsis contains a large set of CASP/CASPL family members (reported as 39 in recent family-scale analyses). (xue2024comparativeanalysisof pages 2-4, barbosa2023directedgrowthand pages 1-2)

2. Gene-specific functional evidence for CASPL1D2 (At3g06390)

2.1 Expression pattern (cell type and developmental timing)

Direct reporter evidence (pCASPL1D2::GUS and pCASPL1D2::GFP-CASPL1D2) shows CASPL1D2 expression in the root endodermis and cells overlying the base of lateral roots, with little/no expression in younger tissues. (champeyroux2019regulationofa pages 4-6)

CASPL1D2 expression is associated with suberized endodermal territories. In the examined roots, expression was described as discontinuous over approximately ~29% of mid-root length and then continuous over approximately ~29% of basal root length, consistent with developmental progression of endodermal suberization. (champeyroux2019regulationofa pages 4-6)

2.2 Subcellular localization

In endodermal cells, CASPL1D2 localizes to the plasma membrane, and notably is reported to be excluded from the CSD (i.e., from the CASP-defined Casparian strip membrane domain itself). This positions CASPL1D2 as a plasma-membrane protein acting in endodermal cells but not as a core component of the CASP scaffold at the CS. (champeyroux2019regulationofa pages 4-6)

2.3 Molecular interactions and putative molecular function

CASPL1D2 was identified among proteins associated with the aquaporin PIP2;1 and shows a physical interaction with PIP2;1 by FRET-FLIM after transient expression in tobacco epidermal cells. Quantitatively, CASPL1D2-GFP lifetime decreased from 2247 ± 12 ps to 2171 ± 6 ps in the presence of PIP2;1-SS-RFP (FRET efficiency 1.9%, P = 4.40 × 10−4), supporting direct or very close association in vivo. (champeyroux2019regulationofa pages 8-10)

In Xenopus oocyte assays used to assess functional regulation of aquaporins, CASPL1D2—unlike CASPL1B1—did not measurably stimulate PIP2;1 water transport under the tested conditions, implying that CASPL1D2’s interaction may be context-dependent (e.g., requires additional partners or post-translational states) or affects properties not captured by this assay. (champeyroux2019regulationofa pages 11-12)

2.4 Mutant/phenotype evidence: suberization and root water transport

Loss-of-function alleles showed strong transcript knockdown; CASPL1D2 mRNA was reduced by >89% in the corresponding mutant line(s), supporting effective disruption. (champeyroux2019regulationofa pages 6-8)

A caspl1d1 caspl1d2 double mutant displayed a modest but significant increase in continuous endodermal suberization (42% continuous suberization vs 36% in control), supporting a weak negative regulatory role for the CASPL1D1/D2 pair in suberization under at least some conditions. (champeyroux2019regulationofa pages 6-8)

Under short treatments, continuous suberization increased to 58% after 6 h ABA in both genotypes, while under NaCl the reported values were ~50% (control) vs 56% (double mutant). (champeyroux2019regulationofa pages 6-8)

Despite these suberization changes, CASPL mutants did not show a robust whole-root hydraulic conductivity phenotype under the tested conditions. In one set of comparisons, ABA decreased hydrostatic root hydraulic conductivity (Lpr-h) similarly in WT and the double mutant (53% vs 49% decrease), while NaCl caused a trend toward stronger inhibition in the double mutant (70% vs 52%). (champeyroux2019regulationofa pages 8-10)

The authors also report no significant changes in solute flow (Js) or biomass measures in caspl mutants under their experimental conditions, consistent with CASPL1D2 contributing at most subtly to root barrier modulation rather than dominating whole-root transport. (champeyroux2019regulationofa pages 4-6)

2.5 Regulatory/pathway context: MYB41-linked stress/endodermis program

CASPL1D2 was reported to be the most highly upregulated gene (~300-fold induction) in MYB41 overexpressors, and MYB41 is part of an endodermal program induced by ABA/salt that activates genes contributing to suberin formation. This strongly supports transcriptional coupling of CASPL1D2 to stress-responsive endodermal barrier remodeling. (champeyroux2019regulationofa pages 6-8)

3. Recent developments (prioritizing 2023–2024) and their implications for CASPL1D2

3.1 Updated mechanistic model of CASP/CSD organization (2023)

Barbosa et al. (Nature Communications, July 2023) provide a key mechanistic update: a full CASP knockout indicates CASPs are not strictly required for the initial appearance of correctly positioned lignin microdomains, but are required for proper organization, membrane–wall adhesion, protein exclusion, and for the directed growth/fusion of microdomains into a continuous CS band via effects on secretory foci dynamics and vesicle tethering factor exclusion. (barbosa2023directedgrowthand pages 1-2, barbosa2023directedgrowthand pages 4-5)

This study includes quantitative and visual documentation of the “string-of-pearls” stage and the fusion failure phenotypes in CASP mutants, supporting a modern framework in which domain organization and secretion control are central. (barbosa2023directedgrowthand pages 2-3, barbosa2023directedgrowthand media fb1faa3e)

3.2 CASPL redundancy testing: CASPL1D2 does not compensate for CASP loss (2023)

To test whether CASPLs could explain residual CS initiation or compensate for CASP loss, Barbosa et al. inspected RNA-seq datasets and identified multiple CASPL1-clade members including CASPL1D2 as upregulated in myb36 or CIF2 conditions. However, adding knockouts of six endodermis-expressed CASPLs (including CASPL1D2) to caspQ (creating an undecuple mutant) did not increase phenotypic severity. This indicates that CASPL1D2 is not redundant with CASP1–5 for early CS microdomain initiation/fusion phenotypes and supports a distinct, likely later or parallel role (e.g., suberized endodermis PM functions). (barbosa2023directedgrowthand pages 3-4, barbosa2023directedgrowthand pages 4-5)

3.3 Consensus terminology and methodological guidance for membrane domains (2024)

The Nature Plants consensus guidelines (August 2024) recommend describing structures like the CSD as polar domains assembled from nanodomains, and emphasize that domains can be interpreted using driver–client relationships (CASPs as drivers vs lignin enzymes as clients), diffusion barriers, and quantitative imaging/biochemical approaches (including proximity labeling and detergent-free nanodisc purification). This provides an authoritative framing for how CASPL1D2 localization (PM but excluded from CSD) should be interpreted in domain terms. (jaillais2024guidelinesfornaming pages 4-6, jaillais2024guidelinesfornaming pages 6-8, jaillais2024guidelinesfornaming pages 8-13)

3.4 2024 family-scale analyses: counts, promoter motifs, and endodermis enrichment

A 2024 comparative bioinformatics analysis reports 39 Arabidopsis CASP/CASPL genes identified via DUF588 (PF04535) HMM approaches and clustered into six subfamilies, and further reports that many CASP/CASPL genes are preferentially expressed in roots and often enriched in endodermal cells. Such family-scale resources contextualize CASPL1D2 as one member of a diversified membrane-protein family associated with diffusion barrier development and stress responsiveness. (xue2024comparativeanalysisof pages 2-4, xue2024comparativeanalysisof pages 1-2, xue2024comparativeanalysisof pages 7-11)

4. Primary functional interpretation (most supported annotation)

4.1 What CASPL1D2 most likely does

The strongest direct evidence supports CASPL1D2 as an endodermis plasma-membrane protein associated with suberized endodermal cells and with physical proximity/interaction to the aquaporin PIP2;1, with a weak negative influence on continuous suberization when CASPL1D2 is disrupted together with CASPL1D1. (champeyroux2019regulationofa pages 4-6, champeyroux2019regulationofa pages 8-10, champeyroux2019regulationofa pages 6-8)

Because CASPL1D2 is excluded from the CSD, it is unlikely to be a core CASP-like scaffold protein directly assembling the Casparian strip membrane domain. Instead, CASPL1D2 likely participates in plasma membrane functions of differentiated/suberized endodermis, potentially modulating aquaporin complex properties or endodermis-specific membrane organization during suberization and stress adaptation. (champeyroux2019regulationofa pages 4-6, champeyroux2019regulationofa pages 11-12)

4.2 What CASPL1D2 does not appear to do (based on current evidence)

• It does not show strong evidence of being required for bulk root hydraulic conductivity under tested conditions, despite its interaction with PIP2;1. (champeyroux2019regulationofa pages 1-2, champeyroux2019regulationofa pages 8-10)
• It does not compensate for CASP1–5 loss in early Casparian strip formation/fusion, based on high-order mutant analysis. (barbosa2023directedgrowthand pages 3-4)

5. Current applications and real-world implementations

Research on CASP/CASPL proteins is increasingly linked to engineering root diffusion barriers to modify nutrient and ion uptake and stress tolerance. For example, mechanistic insights into how membrane scaffolds organize lignin-based barriers inform strategies to strengthen or tune barrier properties (e.g., for salinity resilience) and to interpret endodermis barrier phenotypes in crop improvement research. While CASPL1D2 itself has not yet been directly deployed in applied engineering in the cited studies, its connection to suberized endodermis programs and stress-responsive regulation makes it a plausible candidate for future barrier-modulation strategies, particularly when combined with transcriptional regulators such as MYB41-linked networks. (champeyroux2019regulationofa pages 6-8, barbosa2023directedgrowthand pages 1-2)

6. Expert opinions and synthesis from authoritative sources

Two high-authority sources shape current interpretation:
1) Barbosa et al. 2023 (Nat Commun) emphasize that CASPs function primarily in domain organization, secretion control, and membrane–wall adhesion, rather than being strictly required for initial lignin targeting—reframing the CS as an emergent property of coupled trafficking and membrane domain dynamics. (barbosa2023directedgrowthand pages 1-2, barbosa2023directedgrowthand pages 4-5)
2) Jaillais et al. 2024 (Nat Plants) emphasize a rigorous conceptual vocabulary (polar domains vs nanodomains) and careful methodological standards for claiming “domains,” supporting conservative interpretation of proteins like CASPL1D2 that localize to the PM but are excluded from the CSD. (jaillais2024guidelinesfornaming pages 4-6, jaillais2024guidelinesfornaming pages 6-8)

7. Relevant statistics and recent data highlights

Key quantitative findings directly tied to CASPL1D2 include:
- Expression perturbation: CASPL1D2 transcript reduced >89% in mutant line(s). (champeyroux2019regulationofa pages 6-8)
- Regulatory induction: ~300-fold induction in MYB41 overexpressors. (champeyroux2019regulationofa pages 6-8)
- Suberization phenotype: 42% vs 36% continuous suberization (double mutant vs control); ABA (6 h) 58% both; NaCl ~50% vs 56%. (champeyroux2019regulationofa pages 6-8)
- Protein interaction metric: FRET-FLIM lifetime shift 2247 ± 12 ps → 2171 ± 6 ps, FRET efficiency 1.9%, P = 4.40 × 10−4 (interaction with PIP2;1). (champeyroux2019regulationofa pages 8-10)
- Hydraulic response trends: ABA reduces Lpr-h 53% vs 49% (WT vs double mutant); NaCl 52% vs 70% (trend). (champeyroux2019regulationofa pages 8-10)

For the underlying CS-domain framework (supporting inference): CASP mutants show stalled string-of-pearls progression and reduced lignin foci coverage (reported as ~50% of area at maturity in certain casp mutants/caspQ vs WT), with quantitative particle/area analyses presented in figures. (barbosa2023directedgrowthand pages 2-3, barbosa2023directedgrowthand media fb1faa3e)

8. Visual evidence (CASP/CSD conceptual framework)

Cropped figures from Barbosa et al. (2023) provide direct visual/quantitative evidence for the CASP microdomain “string-of-pearls” progression, fusion into a continuous strip, and mutant failure modes that define the modern mechanistic framework for the CSD. (barbosa2023directedgrowthand media fb1faa3e, barbosa2023directedgrowthand media 0122206e, barbosa2023directedgrowthand media 8b5be675, barbosa2023directedgrowthand media 675ffc01)

9. Evidence summary table

Table: This table summarizes gene-specific and family-level functional annotation evidence for Arabidopsis CASPL1D2/At3g06390, including localization, interactions, phenotypes, regulation, and quantitative findings. It is useful as a compact evidence map showing where direct data exist and where inference depends on broader CASP/CASPL biology.

10. Key references (with dates and URLs)

• Champeyroux C. et al. Regulation of a plant aquaporin by a Casparian strip membrane domain protein-like. Plant, Cell & Environment (Publication month: Mar 2019). https://doi.org/10.1111/pce.13537 (champeyroux2019regulationofa pages 4-6, champeyroux2019regulationofa pages 8-10, champeyroux2019regulationofa pages 6-8)
• Barbosa I.C.R. et al. Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci. Nature Communications (Publication month: Jul 2023). https://doi.org/10.1038/s41467-023-37265-7 (barbosa2023directedgrowthand pages 1-2, barbosa2023directedgrowthand pages 3-4, barbosa2023directedgrowthand media fb1faa3e)
• Jaillais Y. et al. Guidelines for naming and studying plasma membrane domains in plants. Nature Plants (Publication month: Aug 2024). https://doi.org/10.1038/s41477-024-01742-8 (jaillais2024guidelinesfornaming pages 4-6, jaillais2024guidelinesfornaming pages 6-8, jaillais2024guidelinesfornaming pages 8-13)
• Xue B. et al. Comparative Analysis of Casparian Strip Membrane Domain Protein Family in Oryza sativa and Arabidopsis thaliana. International Journal of Molecular Sciences (Publication month: Sep 2024). https://doi.org/10.3390/ijms25189858 (xue2024comparativeanalysisof pages 2-4, xue2024comparativeanalysisof pages 1-2, xue2024comparativeanalysisof pages 7-11)

References

1. (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 19 citations.

2. (xue2024comparativeanalysisof pages 2-4): Baoping Xue, Zicong Liang, Yue Liu, Dongyang Li, Peng Cao, and Chang Liu. Comparative analysis of casparian strip membrane domain protein family in oryza sativa (l.) and arabidopsis thaliana (l.). International Journal of Molecular Sciences, 25:9858, Sep 2024. URL: https://doi.org/10.3390/ijms25189858, doi:10.3390/ijms25189858. This article has 5 citations.

3. (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 33 citations and is from a highest quality peer-reviewed journal.

4. (jaillais2024guidelinesfornaming pages 6-8): Yvon Jaillais, Emmanuelle Bayer, Dominique C. Bergmann, Miguel A. Botella, Yohann Boutté, Tolga O. Bozkurt, Marie-Cecile Caillaud, Véronique Germain, Guido Grossmann, Ingo Heilmann, Piers A. Hemsley, Charlotte Kirchhelle, Alexandre Martinière, Yansong Miao, Sebastien Mongrand, Sabine Müller, Lise C. Noack, Yoshihisa Oda, Thomas Ott, Xue Pan, Roman Pleskot, Martin Potocky, Stéphanie Robert, Clara Sanchez Rodriguez, Françoise Simon-Plas, Eugenia Russinova, Daniel Van Damme, Jaimie M. Van Norman, Dolf Weijers, Shaul Yalovsky, Zhenbiao Yang, Enric Zelazny, and Julien Gronnier. Guidelines for naming and studying plasma membrane domains in plants. Nature plants, 10:1172-1183, Aug 2024. URL: https://doi.org/10.1038/s41477-024-01742-8, doi:10.1038/s41477-024-01742-8. This article has 48 citations and is from a highest quality peer-reviewed journal.

5. (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 33 citations and is from a highest quality peer-reviewed journal.

6. (jaillais2024guidelinesfornaming pages 4-6): Yvon Jaillais, Emmanuelle Bayer, Dominique C. Bergmann, Miguel A. Botella, Yohann Boutté, Tolga O. Bozkurt, Marie-Cecile Caillaud, Véronique Germain, Guido Grossmann, Ingo Heilmann, Piers A. Hemsley, Charlotte Kirchhelle, Alexandre Martinière, Yansong Miao, Sebastien Mongrand, Sabine Müller, Lise C. Noack, Yoshihisa Oda, Thomas Ott, Xue Pan, Roman Pleskot, Martin Potocky, Stéphanie Robert, Clara Sanchez Rodriguez, Françoise Simon-Plas, Eugenia Russinova, Daniel Van Damme, Jaimie M. Van Norman, Dolf Weijers, Shaul Yalovsky, Zhenbiao Yang, Enric Zelazny, and Julien Gronnier. Guidelines for naming and studying plasma membrane domains in plants. Nature plants, 10:1172-1183, Aug 2024. URL: https://doi.org/10.1038/s41477-024-01742-8, doi:10.1038/s41477-024-01742-8. This article has 48 citations and is from a highest quality peer-reviewed journal.

7. (jaillais2024guidelinesfornaming pages 8-13): Yvon Jaillais, Emmanuelle Bayer, Dominique C. Bergmann, Miguel A. Botella, Yohann Boutté, Tolga O. Bozkurt, Marie-Cecile Caillaud, Véronique Germain, Guido Grossmann, Ingo Heilmann, Piers A. Hemsley, Charlotte Kirchhelle, Alexandre Martinière, Yansong Miao, Sebastien Mongrand, Sabine Müller, Lise C. Noack, Yoshihisa Oda, Thomas Ott, Xue Pan, Roman Pleskot, Martin Potocky, Stéphanie Robert, Clara Sanchez Rodriguez, Françoise Simon-Plas, Eugenia Russinova, Daniel Van Damme, Jaimie M. Van Norman, Dolf Weijers, Shaul Yalovsky, Zhenbiao Yang, Enric Zelazny, and Julien Gronnier. Guidelines for naming and studying plasma membrane domains in plants. Nature plants, 10:1172-1183, Aug 2024. URL: https://doi.org/10.1038/s41477-024-01742-8, doi:10.1038/s41477-024-01742-8. This article has 48 citations and is from a highest quality peer-reviewed journal.

8. (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 19 citations.

9. (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 19 citations.

10. (champeyroux2019regulationofa pages 11-12): 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 19 citations.

11. (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 19 citations.

12. (barbosa2023directedgrowthand pages 4-5): 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 33 citations and is from a highest quality peer-reviewed journal.

13. (barbosa2023directedgrowthand media fb1faa3e): 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 33 citations and is from a highest quality peer-reviewed journal.

14. (barbosa2023directedgrowthand pages 3-4): 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 33 citations and is from a highest quality peer-reviewed journal.

15. (xue2024comparativeanalysisof pages 1-2): Baoping Xue, Zicong Liang, Yue Liu, Dongyang Li, Peng Cao, and Chang Liu. Comparative analysis of casparian strip membrane domain protein family in oryza sativa (l.) and arabidopsis thaliana (l.). International Journal of Molecular Sciences, 25:9858, Sep 2024. URL: https://doi.org/10.3390/ijms25189858, doi:10.3390/ijms25189858. This article has 5 citations.

16. (xue2024comparativeanalysisof pages 7-11): Baoping Xue, Zicong Liang, Yue Liu, Dongyang Li, Peng Cao, and Chang Liu. Comparative analysis of casparian strip membrane domain protein family in oryza sativa (l.) and arabidopsis thaliana (l.). International Journal of Molecular Sciences, 25:9858, Sep 2024. URL: https://doi.org/10.3390/ijms25189858, doi:10.3390/ijms25189858. This article has 5 citations.

17. (barbosa2023directedgrowthand media 0122206e): 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 33 citations and is from a highest quality peer-reviewed journal.

18. (barbosa2023directedgrowthand media 8b5be675): 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 33 citations and is from a highest quality peer-reviewed journal.

19. (barbosa2023directedgrowthand media 675ffc01): 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 33 citations and is from a highest quality peer-reviewed journal.

20. (xue2024comparativeanalysisof pages 15-17): Baoping Xue, Zicong Liang, Yue Liu, Dongyang Li, Peng Cao, and Chang Liu. Comparative analysis of casparian strip membrane domain protein family in oryza sativa (l.) and arabidopsis thaliana (l.). International Journal of Molecular Sciences, 25:9858, Sep 2024. URL: https://doi.org/10.3390/ijms25189858, doi:10.3390/ijms25189858. This article has 5 citations.

Artifacts

• Edison artifact artifact-00
  

Citations

1. barbosa2023directedgrowthand pages 1-2
2. jaillais2024guidelinesfornaming pages 6-8
3. champeyroux2019regulationofa pages 4-6
4. champeyroux2019regulationofa pages 8-10
5. champeyroux2019regulationofa pages 11-12
6. champeyroux2019regulationofa pages 6-8
7. barbosa2023directedgrowthand pages 3-4
8. champeyroux2019regulationofa pages 1-2
9. xue2024comparativeanalysisof pages 2-4
10. barbosa2023directedgrowthand pages 2-3
11. jaillais2024guidelinesfornaming pages 4-6
12. jaillais2024guidelinesfornaming pages 8-13
13. barbosa2023directedgrowthand pages 4-5
14. xue2024comparativeanalysisof pages 1-2
15. xue2024comparativeanalysisof pages 7-11
16. xue2024comparativeanalysisof pages 15-17
17. https://doi.org/10.1111/pce.13537;
18. https://doi.org/10.3390/ijms25189858;
19. https://doi.org/10.1038/s41467-023-37265-7
20. https://doi.org/10.3390/ijms25189858
21. https://doi.org/10.1111/pce.13537
22. https://doi.org/10.1038/s41467-023-37265-7;
23. https://doi.org/10.1038/s41477-024-01742-8
24. https://doi.org/10.1111/pce.13537,
25. https://doi.org/10.3390/ijms25189858,
26. https://doi.org/10.1038/s41467-023-37265-7,
27. https://doi.org/10.1038/s41477-024-01742-8,