Evidence map›Paper›PMID 38842334›Full record

ArticleThe Plant cell2024

PLASMODESMATA-LOCATED PROTEIN 6 regulates plasmodesmal function in Arabidopsis vasculature.

Zhongpeng Li, Su-Ling Liu, Christian Montes-Serey, Justin W Walley, Kyaw Aung

Abstract read
In one paragraph

Article in The Plant cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

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  17. Review
  18. A PDLP-NHL3 complex integrates plasmodesmal immune signaling cascades.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Zhongpeng LiDepartment of Genetics, Development, and Cell Biology, Iowa State University, Ames, IA 50011, USA.ORCID 0000-0001-7524-7276
Su-Ling LiuDepartment of Genetics, Development, and Cell Biology, Iowa State University, Ames, IA 50011, USA.ORCID 0000-0002-1213-110X
Christian Montes-SereyDepartment of Plant Pathology, Entomology and Microbiology, Iowa State University, Ames, IA 50011, USA.ORCID 0000-0003-1249-2308
Justin W WalleyDepartment of Plant Pathology, Entomology and Microbiology, Iowa State University, Ames, IA 50011, USA.ORCID 0000-0001-7553-2237
Kyaw AungDepartment of Genetics, Development, and Cell Biology, Iowa State University, Ames, IA 50011, USA.ORCID 0000-0002-4728-2522

Funding

A bacterial effector protein modulates host cell-to-cell communicationR00GM115766 · NIGMS · IOWA STATE UNIVERSITY · PI AUNG, KYAW · 2019 to 2021
$747k
Hatch Act IOW04308ISU Crop Bioengineering CenterISU Plant Sciences InstituteNational Science Foundation MCB2339067NIGMS NIH HHS R00 GM115766NIGMS NIH HHS R00GM115766
6 · The paper itself

Abstract

Plasmodesmata connect adjoining plant cells, allowing molecules to move between the connected cells for communication and sharing resources. It has been well established that the plant polysaccharide callose is deposited at plasmodesmata, regulating their aperture and function. Among proteins involved in maintaining callose homeostasis, PLASMODESMATA-LOCATED PROTEINSs (PDLPs) promote callose deposition at plasmodesmata. This study explored the function of PDLP5 and PDLP6 in different cell types. We discovered that PDLP5 and PDLP6 are expressed in nonoverlapping cell types in Arabidopsis (Arabidopsis thaliana). The overexpression of PDLP5 and PDLP6 results in the overaccumulation of plasmodesmal callose at different cell interfaces, indicating that PDLP5 and PDLP6 are active in different cell types. We also observed 2 distinct patterns of starch accumulation in mature leaves of PDLP5 and PDLP6 overexpressors. An enzyme-catalyzed proximity labeling approach was used to identify putative functional partners of the PDLPs. We identified SUCROSE SYNTHASE 6 (SUS6) as a functional partner of PDLP6 in the vasculature. We further demonstrated that PDLP6 physically and genetically interacts with SUS6. In addition, CALLOSE SYNTHASE 7 (CALS7) physically interacts with SUS6 and PDLP6. Genetic interaction studies showed that CALS7 is required for PDLP6 function. We propose that PDLP6 functions with SUS6 and CALS7 in the vasculature to regulate plasmodesmal function.

Indexed as

ArabidopsisArabidopsis ProteinsGlucansPlasmodesmataGene Expression Regulation, PlantGlucosyltransferasesMembrane ProteinsPlant LeavesPlants, Genetically ModifiedStarchArabidopsis ProteinscalloseGlucansGlucosyltransferasesMembrane ProteinsPDLP5 protein, ArabidopsisStarch

Identifiers

PMID38842334
PMCPMC11371196

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.