Evidence map›Paper›PMID 31324141›Full record

ArticleBMC plant biology2019

Proximity-dependent biotinylation screening identifies NbHYPK as a novel interacting partner of ATG8 in plants.

Mercy W Macharia, Wilfred Y Z Tan, Prem P Das, Naweed I Naqvi, Sek-Man Wong

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 24 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

5 authors at 2 institutions in 2 countries.

Mercy W MachariaDepartment of Biological Sciences, National University of Singapore, Singapore, 119543, Singapore.
Wilfred Y Z TanDepartment of Biological Sciences, National University of Singapore, Singapore, 119543, Singapore.
Prem P DasDepartment of Biological Sciences, National University of Singapore, Singapore, 119543, Singapore.
Naweed I NaqviDepartment of Biological Sciences, National University of Singapore, Singapore, 119543, Singapore.
Sek-Man WongDepartment of Biological Sciences, National University of Singapore, Singapore, 119543, Singapore. dbswsm@nus.edu.sg.ORCID http://orcid.org/0000-0002-4620-3706
National University of Singapore · SGTemasek Life Sciences Laboratory · SG

Funding

Ministry of Education R-154-000-B23-114National Natural Science Foundation of China 31872639National University of Singapore SINGA ScholarshipSuzhou Municipal Science and Technology Bureau SNG2018039Temasek Life Sciences Laboratory Intramural funding
6 · The paper itself

Abstract

backgroundAutophagy is a conserved, highly-regulated catabolic process that plays important roles in growth, development and innate immunity in plants. In this study, we compared the rate of autophagy induction in Nicotiana benthamiana plants infected with Tobacco mosaic virus or the TMV 24A + UPD mutant variant, which replicates at a faster rate and induces more severe symptoms. Using a BirA* tag and proximity-dependent biotin identification (BioID) analysis, we identified host proteins that interact with the core autophagy protein, ATG8 in TMV 24A + UPD infected plants. By combining the use of a fast replicating TMV mutant and an in vivo protein-protein screening technique, we were able to gain functional insight into the role of autophagy in a compatible virus-host interaction.

resultsOur study revealed an increased autophagic flux induced by TMV 24A + UPD, as compared to TMV in N. benthamiana. Analysis of the functional proteome associated with ATG8 revealed a total of 67 proteins, 16 of which are known to interact with ATG8 or its orthologs in mammalian and yeast systems. The interacting proteins were categorized into four functional groups: immune system process, response to ROS, sulphur amino acid metabolism and calcium signalling. Due to the presence of an ubiquitin-associated (UBA) domain, which is demonstrated to interact with ATG8, the Huntingtin-interacting protein K-like (HYPK) was selected for validation of the physical interaction and function. We used yeast two hybrid (Y2H), bimolecular fluorescence complementation (BiFC) and subcellular localization to validate the ATG8-HYPK interaction. Subsequent down-regulation of ATG8 by virus-induced gene silencing (VIGS) showed enhanced TMV symptoms, suggesting a protective role for autophagy during TMV 24A + UPD infection.

conclusionThis study presents the use of BioID as a suitable method for screening ATG8 interacting proteins in planta. We have identified many putative binding partners of ATG8 during TMV 24A + UPD infection in N. benthamiana plants. In addition, we have verified that NbHYPK is an interacting partner of ATG8. We infer that autophagy plays a protective role in TMV 24A + UPD infected plants.

Indexed as

AutophagosomesAutophagyAutophagy-Related Protein 8 FamilyBiotinylationNicotianaPlant DiseasesPlant ImmunityPlant ProteinsTobacco Mosaic VirusAutophagy-Related Protein 8 FamilyPlant ProteinsATG8AutophagyBioIDHYPKProtein-protein interactionTMVTMV 24A + UPD

Identifiers

PMID31324141
PMCPMC6642529
OpenAlexW2964280833

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.