Evidence map›Paper›PMID 26166780›Full record

ArticleCurrent biology : CB2015

Synaptotagmin SYTA forms ER-plasma membrane junctions that are recruited to plasmodesmata for plant virus movement.

Amit Levy, Judy Y Zheng, Sondra G Lazarowitz

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed, 1 pooled it
26.9field-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

93 citing papers in PubMed, 1 synthesis or guideline pooled it, 170 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. 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
  6. Review
  7. Article
  8. Article
  9. Review
  10. Cellular Partners of Tobamoviral Movement Proteins.International journal of molecular sciences · 2025
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Studying Plant ER-PM Contact Site Localized Proteins Using Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  20. Article

33 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Amit LevyDepartment of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY 14853, USA.
Judy Y ZhengDepartment of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY 14853, USA.
Sondra G LazarowitzDepartment of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY 14853, USA. Electronic address: sgl5@cornell.edu.
Cornell University · US

Funding

Synaptotagmin function in virus movement and plant developmentR01AI066054 · NIAID · CORNELL UNIVERSITY · PI LAZAROWITZ, SONDRA G · 2007 to 2010
$1.4M
NIAID NIH HHS AI-066054NIAID NIH HHS R01 AI066054
6 · The paper itself

Abstract

Metazoan synaptotagmins are Ca(2+) sensors that regulate exocytosis and endocytosis in various cell types, notably in nerve and neuroendocrine cells [1, 2]. Recently, the structurally related extended synaptotagmins were shown to tether the cortical ER to the plasma membrane in human and yeast cells to maintain ER morphology and stabilize ER-plasma membrane (ER-PM) contact sites for intracellular lipid and Ca(2+) signaling [3, 4]. The Arabidopsis synaptotagmin SYTA regulates endocytosis and the ability of plant virus movement proteins (MPs) to alter plasmodesmata to promote virus cell-to-cell transport [5, 6]. Yet how MPs modify plasmodesmata, the cellular functions of SYTA and how these aid MP activity, and the proteins essential to form plant cell ER-PM contact sites remain unknown. We addressed these questions using an Arabidopsis SYTA knockdown line syta-1 and a Tobamovirus movement protein MP(TVCV) [5, 7]. We report here that SYTA localized to ER-PM contact sites. These sites were depleted and the ER network collapsed in syta-1, and both reformed upon rescue with SYTA. MP(TVCV) accumulation in plasmodesmata, but not secretory trafficking, was also inhibited in syta-1. During infection, MP(TVCV) recruited SYTA to plasmodesmata, and SYTA and the cortical ER were subsequently remodeled to form viral replication sites adjacent to plasmodesmata in which MP(TVCV) and SYTA directly interacted caged within ER membrane. SYTA also accumulated in plasmodesmata active in MP(TVCV) transport. Our findings show that SYTA is essential to form ER-PM contact sites and suggest that MPs interact with SYTA to recruit these sites to alter plasmodesmata for virus cell-to-cell movement.

Indexed as

ArabidopsisArabidopsis ProteinsBiological TransportCell MembraneEndoplasmic ReticulumPlant Viral Movement ProteinsPlasmodesmataSynaptotagmin ISynaptotagminsTobamovirusVirus ReplicationArabidopsis ProteinsAt2g20990 protein, ArabidopsisPlant Viral Movement ProteinsSynaptotagmin ISynaptotagmins

Identifiers

PMID26166780
PMCPMC4526382
OpenAlexW1691688704

What OpenQuestion holds

Textmetadata
LicenceTDM
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.