Evidence map›Paper›PMID 11591731›Full record

ArticleThe Journal of cell biology2001

Functional characterization of the KNOLLE-interacting t-SNARE AtSNAP33 and its role in plant cytokinesis.

M Heese, X Gansel, L Sticher, P Wick, M Grebe, F Granier, G Jurgens

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

70 citing papers in PubMed, 176 citations in OpenAlex.

  1. Article
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  6. Roles of the ArabidopsisInternational journal of molecular sciences · 2024
    Article
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  15. Article
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  19. GhSNAP33, a t-SNARE Protein FromFrontiers in plant science · 2018
    Article
  20. Activation of disease resistance againstHorticulture research · 2018
    Article

10 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

7 authors at 3 institutions in 3 countries.

M HeeseZentrum für Molekularbiologie der Pflanzen, Universität Tübingen, D-72076 Tübingen, Germany.
X Gansel
L Sticher
P Wick
M Grebe
F Granier
G Jurgens
University of Fribourg · CHUniversity of Tübingen · DEDépartement Santé des Plantes et Environnement · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytokinesis requires membrane fusion during cleavage-furrow ingression in animals and cell plate formation in plants. In Arabidopsis, the Sec1 homologue KEULE (KEU) and the cytokinesis-specific syntaxin KNOLLE (KN) cooperate to promote vesicle fusion in the cell division plane. Here, we characterize AtSNAP33, an Arabidopsis homologue of the t-SNARE SNAP25, that was identified as a KN interactor in a yeast two-hybrid screen. AtSNAP33 is a ubiquitously expressed membrane-associated protein that accumulated at the plasma membrane and during cell division colocalized with KN at the forming cell plate. A T-DNA insertion in the AtSNAP33 gene caused loss of AtSNAP33 function, resulting in a lethal dwarf phenotype. atsnap33 plantlets gradually developed large necrotic lesions on cotyledons and rosette leaves, resembling pathogen-induced cellular responses, and eventually died before flowering. In addition, mutant seedlings displayed cytokinetic defects, and atsnap33 in combination with the cytokinesis mutant keu was embryo lethal. Analysis of the Arabidopsis genome revealed two further SNAP25-like proteins that also interacted with KN in the yeast two-hybrid assay. Our results suggest that AtSNAP33, the first SNAP25 homologue characterized in plants, is involved in diverse membrane fusion processes, including cell plate formation, and that AtSNAP33 function in cytokinesis may be replaced partially by other SNAP25 homologues.

Indexed as

Cell DivisionPlant ProteinsVesicular Transport ProteinsAmino Acid SequenceArabidopsisArabidopsis ProteinsCarrier ProteinsCell Cycle ProteinsIntracellular MembranesMembrane FusionMembrane ProteinsMolecular Sequence DataMutagenesis, InsertionalMutationNerve Tissue ProteinsPhenotypeArabidopsis ProteinsAT1G12360 protein, ArabidopsisCarrier ProteinsCell Cycle ProteinsKNOLLE protein, ArabidopsisMembrane ProteinsNerve Tissue ProteinsPlant ProteinsQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsSNAP33 protein, ArabidopsisSynaptosomal-Associated Protein 25Vesicular Transport Proteins

Identifiers

PMID11591731
PMCPMC2198836
OpenAlexW2011610941

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.