Evidence map›Paper›PMID 34618135›Full record

ArticlePlant physiology2021

A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for the begomovirus CabLCV.

Bianca Castro Gouveia-Mageste, Laura Gonçalves Costa Martins, Maximiller Dal-Bianco, João Paulo Batista Machado, José Cleydson Ferreira da Silva, Alice Y Kim, Junshi Yazaki, Anésia Aparecida Dos Santos, Joseph R Ecker, Elizabeth Pacheco Batista Fontes

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.3field-weighted citation impact, top 9% of its field
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

11 citing papers in PubMed, 21 citations in OpenAlex.

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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

10 authors at 2 institutions in 3 countries.

Bianca Castro Gouveia-MagesteNational Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.
Laura Gonçalves Costa MartinsNational Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.
Maximiller Dal-BiancoNational Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.
João Paulo Batista MachadoNational Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.
José Cleydson Ferreira da SilvaNational Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.
Alice Y KimGenomic Analysis Laboratory, Plant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037, USA.
Junshi YazakiGenomic Analysis Laboratory, Plant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037, USA.ORCID 0000-0002-0697-8320
Anésia Aparecida Dos SantosNational Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.
Joseph R EckerHoward Hughes Medical Institute and Plant Biology Laboratory, The Salk Institute of Biological Studies, La Jolla, California 92037, USA.ORCID 0000-0001-5799-5895
Elizabeth Pacheco Batista FontesNational Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.ORCID 0000-0002-7986-1369
Universidade Federal de Viçosa · BRSalk Institute for Biological Studies · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Because of limited free diffusion in the cytoplasm, viruses must use active transport mechanisms to move intracellularly. Nevertheless, how the plant single-stranded DNA begomoviruses hijack the host intracytoplasmic transport machinery to move from the nucleus to the plasmodesmata remains enigmatic. Here, we identified nuclear shuttle protein (NSP)-interacting proteins from Arabidopsis (Arabidopsis thaliana) by probing a protein microarray and demonstrated that the cabbage leaf curl virus NSP, a facilitator of the nucleocytoplasmic trafficking of viral (v)DNA, interacts in planta with an endosomal vesicle-localized, plant-specific syntaxin-6 protein, designated NSP-interacting syntaxin domain-containing protein (NISP). NISP displays a proviral function, unlike the syntaxin-6 paralog AT2G18860 that failed to interact with NSP. Consistent with these findings, nisp-1 mutant plants were less susceptible to begomovirus infection, a phenotype reversed by NISP complementation. NISP-overexpressing lines accumulated higher levels of vDNA than wild-type. Furthermore, NISP interacted with an NSP-interacting GTPase (NIG) involved in NSP-vDNA nucleocytoplasmic translocation. The NISP-NIG interaction was enhanced by NSP. We also showed that endosomal NISP associates with vDNA. NISP may function as a docking site for recruiting NIG and NSP into endosomes, providing a mechanism for the intracytoplasmic translocation of the NSP-vDNA complex toward and from the cell periphery.

Indexed as

ArabidopsisBegomovirusArabidopsis ProteinsCell NucleusQa-SNARE ProteinsArabidopsis ProteinsAT4G30240 protein, ArabidopsisQa-SNARE Proteins

Identifiers

PMID34618135
PMCPMC8418432
OpenAlexW3167146217

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.