Evidence map›Paper›PMID 34470819›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Plasma membrane phospholipid signature recruits the plant exocyst complex via the EXO70A1 subunit.

Lukáš Synek, Roman Pleskot, Juraj Sekereš, Natalia Serrano, Nemanja Vukašinović, Jitka Ortmannová, Martina Klejchová, Přemysl Pejchar, Klára Batystová, Malgorzata Gutkowska and 6 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Genome-wide identification of theFrontiers in plant science · 2026
    Article
  6. Article
  7. Preassembly and independent trafficking of the exocyst complex inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Split-YFP-coupled interaction-dependent TurboID identifies new functions of basal cell polarity inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. The exocyst in context.Biochemical Society transactions · 2024
    Review
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

16 authors at 4 institutions in 2 countries.

Lukáš SynekInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.ORCID 0000-0003-2111-2450
Roman PleskotInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.ORCID 0000-0003-0436-9748
Juraj SekerešInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.
Natalia SerranoInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.ORCID 0000-0002-1110-3182
Nemanja VukašinovićInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.
Jitka OrtmannováInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.
Martina KlejchováInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.ORCID 0000-0002-1446-0791
Přemysl PejcharInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.
Klára BatystováInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.ORCID 0000-0003-1537-6310
Malgorzata GutkowskaInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, Poland.ORCID 0000-0001-6584-7964
Edita Janková-DrdováInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.ORCID 0000-0001-7928-981X
Vedrana MarkovićInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.ORCID 0000-0002-0310-5102
Tamara PečenkováInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic.ORCID 0000-0003-4743-2225
Jiří ŠantrůčekDepartment of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology, 166 28 Prague, Czech Republic.ORCID 0000-0003-0832-757X
Viktor ŽárskýInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic; zarsky@ueb.cas.cz potocky@ueb.cas.cz.ORCID 0000-0002-5301-0339
Martin PotockýInstitute of Experimental Botany, Czech Academy of Sciences, 165 02 Prague, Czech Republic; zarsky@ueb.cas.cz potocky@ueb.cas.cz.ORCID 0000-0002-3699-7549
Czech Academy of Sciences, Institute of Experimental Botany · CZCharles University · CZInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLUniversity of Chemistry and Technology, Prague · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polarized exocytosis is essential for many vital processes in eukaryotic cells, where secretory vesicles are targeted to distinct plasma membrane domains characterized by their specific lipid-protein composition. Heterooctameric protein complex exocyst facilitates the vesicle tethering to a target membrane and is a principal cell polarity regulator in eukaryotes. The architecture and molecular details of plant exocyst and its membrane recruitment have remained elusive. Here, we show that the plant exocyst consists of two modules formed by SEC3-SEC5-SEC6-SEC8 and SEC10-SEC15-EXO70-EXO84 subunits, respectively, documenting the evolutionarily conserved architecture within eukaryotes. In contrast to yeast and mammals, the two modules are linked by a plant-specific SEC3-EXO70 interaction, and plant EXO70 functionally dominates over SEC3 in the exocyst recruitment to the plasma membrane. Using an interdisciplinary approach, we found that the C-terminal part of EXO70A1, the canonical EXO70 isoform in

Indexed as

ArabidopsisArabidopsis ProteinsCell MembraneCell PolarityCytoplasmExocytosisPhospholipidsProteomicsArabidopsis ProteinsEXO70A1 protein, ArabidopsisPhospholipidscell polarityEXO70A1exocystphospholipidsplasma membrane

Identifiers

PMID34470819
PMCPMC8433549
OpenAlexW3196518801

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.