Evidence map›Paper›PMID 26353761›Full record

ArticlePlant physiology2015

Reticulomics: Protein-Protein Interaction Studies with Two Plasmodesmata-Localized Reticulon Family Proteins Identify Binding Partners Enriched at Plasmodesmata, Endoplasmic Reticulum, and the Plasma Membrane.

Verena Kriechbaumer, Stanley W Botchway, Susan E Slade, Kirsten Knox, Lorenzo Frigerio, Karl Oparka, Chris Hawes

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
19.1field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Review
  3. FRET-FLIM: Unveiling Transcription Factor Interactions in Plants.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Concerted transport and phosphorylation of diacylglycerol at ER-PM contact sites regulate phospholipid dynamics during stress.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. The Extended Synaptotagmins ofPlants (Basel, Switzerland) · 2025
    Review
  6. Review
  7. Cellular Partners of Tobamoviral Movement Proteins.International journal of molecular sciences · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Immunoprecipitation and FRET-FLIM to Determine Metabolons on the Plant ER.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  15. Make It Shine: Labelling the ER for Light and Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Verena KriechbaumerPlant Cell Biology, Biological and Medical Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom (V.K., C.H.);Central Laser Facility, Science and Technology Facilities Council (STFC) Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0QX, United Kingdom (S.W.B.);Warwickshire Private Hospital (WPH) Proteomics Facility Research Technology Platform (S.E.S.) and School of Life Sciences (S.E.S., L.F.), University of Warwick, Coventry CV4 7AL, United Kingdom; andInstitute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom (K.K., K.O.) vkriechbaumer@brookes.ac.uk.ORCID http://orcid.org/0000-0003-3782-5834
Stanley W BotchwayPlant Cell Biology, Biological and Medical Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom (V.K., C.H.);Central Laser Facility, Science and Technology Facilities Council (STFC) Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0QX, United Kingdom (S.W.B.);Warwickshire Private Hospital (WPH) Proteomics Facility Research Technology Platform (S.E.S.) and School of Life Sciences (S.E.S., L.F.), University of Warwick, Coventry CV4 7AL, United Kingdom; andInstitute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom (K.K., K.O.).ORCID http://orcid.org/0000-0002-3268-9303
Susan E SladePlant Cell Biology, Biological and Medical Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom (V.K., C.H.);Central Laser Facility, Science and Technology Facilities Council (STFC) Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0QX, United Kingdom (S.W.B.);Warwickshire Private Hospital (WPH) Proteomics Facility Research Technology Platform (S.E.S.) and School of Life Sciences (S.E.S., L.F.), University of Warwick, Coventry CV4 7AL, United Kingdom; andInstitute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom (K.K., K.O.).ORCID http://orcid.org/0000-0002-0538-1477
Kirsten KnoxPlant Cell Biology, Biological and Medical Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom (V.K., C.H.);Central Laser Facility, Science and Technology Facilities Council (STFC) Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0QX, United Kingdom (S.W.B.);Warwickshire Private Hospital (WPH) Proteomics Facility Research Technology Platform (S.E.S.) and School of Life Sciences (S.E.S., L.F.), University of Warwick, Coventry CV4 7AL, United Kingdom; andInstitute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom (K.K., K.O.).
Lorenzo FrigerioPlant Cell Biology, Biological and Medical Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom (V.K., C.H.);Central Laser Facility, Science and Technology Facilities Council (STFC) Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0QX, United Kingdom (S.W.B.);Warwickshire Private Hospital (WPH) Proteomics Facility Research Technology Platform (S.E.S.) and School of Life Sciences (S.E.S., L.F.), University of Warwick, Coventry CV4 7AL, United Kingdom; andInstitute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom (K.K., K.O.).ORCID http://orcid.org/0000-0003-4100-6022
Karl OparkaPlant Cell Biology, Biological and Medical Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom (V.K., C.H.);Central Laser Facility, Science and Technology Facilities Council (STFC) Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0QX, United Kingdom (S.W.B.);Warwickshire Private Hospital (WPH) Proteomics Facility Research Technology Platform (S.E.S.) and School of Life Sciences (S.E.S., L.F.), University of Warwick, Coventry CV4 7AL, United Kingdom; andInstitute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom (K.K., K.O.).
Chris HawesPlant Cell Biology, Biological and Medical Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom (V.K., C.H.);Central Laser Facility, Science and Technology Facilities Council (STFC) Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0QX, United Kingdom (S.W.B.);Warwickshire Private Hospital (WPH) Proteomics Facility Research Technology Platform (S.E.S.) and School of Life Sciences (S.E.S., L.F.), University of Warwick, Coventry CV4 7AL, United Kingdom; andInstitute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom (K.K., K.O.).ORCID http://orcid.org/0000-0003-4856-7690
Science and Technology Facilities Council · GBOxford Brookes University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J004987/1Biotechnology and Biological Sciences Research Council BB/J005959/1
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is a ubiquitous organelle that plays roles in secretory protein production, folding, quality control, and lipid biosynthesis. The cortical ER in plants is pleomorphic and structured as a tubular network capable of morphing into flat cisternae, mainly at three-way junctions, and back to tubules. Plant reticulon family proteins (RTNLB) tubulate the ER by dimerization and oligomerization, creating localized ER membrane tensions that result in membrane curvature. Some RTNLB ER-shaping proteins are present in the plasmodesmata (PD) proteome and may contribute to the formation of the desmotubule, the axial ER-derived structure that traverses primary PD. Here, we investigate the binding partners of two PD-resident reticulon proteins, RTNLB3 and RTNLB6, that are located in primary PD at cytokinesis in tobacco (Nicotiana tabacum). Coimmunoprecipitation of green fluorescent protein-tagged RTNLB3 and RTNLB6 followed by mass spectrometry detected a high percentage of known PD-localized proteins as well as plasma membrane proteins with putative membrane-anchoring roles. Förster resonance energy transfer by fluorescence lifetime imaging microscopy assays revealed a highly significant interaction of the detected PD proteins with the bait RTNLB proteins. Our data suggest that RTNLB proteins, in addition to a role in ER modeling, may play important roles in linking the cortical ER to the plasma membrane.

Indexed as

Arabidopsis ProteinsBiological TransportCell MembraneEndoplasmic ReticulumGene ExpressionGreen Fluorescent ProteinsImmunoprecipitationMembrane ProteinsNicotianaPlasmodesmataProtein Interaction MappingProteomicsArabidopsis ProteinsGreen Fluorescent ProteinsMembrane Proteinsreticulon-like protein B6, ArabidopsisRTNLB3 protein, Arabidopsis

Identifiers

PMID26353761
PMCPMC4634090
OpenAlexW1945106209

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.