Evidence map›Paper›PMID 30709970›Full record

ArticleJournal of cell science2019

A SEPT1-based scaffold is required for Golgi integrity and function.

Kyungyeun Song, Claudia Gras, Gabrielle Capin, Niclas Gimber, Martin Lehmann, Saif Mohd, Dmytro Puchkov, Maria Rödiger, Ilka Wilhelmi, Oliver Daumke and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

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  12. Quantitative Flow Cytometry-Based Assays for Measuring Constitutive Secretion.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Unlocking Golgi: Why Does Morphology Matter?Biochemistry. Biokhimiia · 2019
    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

13 authors at 4 institutions in 1 country.

Kyungyeun SongLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) Berlin, Molecular Pharmacology and Cell Biology, 13125 Berlin, Germany.ORCID 0000-0003-3569-2310
Claudia GrasLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) Berlin, Molecular Pharmacology and Cell Biology, 13125 Berlin, Germany.ORCID 0000-0002-2845-4181
Gabrielle CapinLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) Berlin, Molecular Pharmacology and Cell Biology, 13125 Berlin, Germany.
Niclas GimberCharité Universitätsmedizin Berlin, Advanced Medical Bioimaging Core Facility - AMBIO, 10117 Berlin, Germany.
Martin LehmannLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) Berlin, Cellular Imaging Facility, 13125 Berlin, Germany.
Saif MohdMax-Delmbrück-Centrum für Molekulare Medizin, 13125 Berlin, Germany.
Dmytro PuchkovLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) Berlin, Cellular Imaging Facility, 13125 Berlin, Germany.
Maria RödigerDeutsches Institut für Ernährungsforschung, Potsdam Rehbrücke, and German Center for Diabetes Research (DZD), München-Neuherberg, 14558 Potsdam-Rehbrücke, Germany.
Ilka WilhelmiDeutsches Institut für Ernährungsforschung, Potsdam Rehbrücke, and German Center for Diabetes Research (DZD), München-Neuherberg, 14558 Potsdam-Rehbrücke, Germany.
Oliver DaumkeMax-Delmbrück-Centrum für Molekulare Medizin, 13125 Berlin, Germany.
Jan SchmoranzerCharité Universitätsmedizin Berlin, Advanced Medical Bioimaging Core Facility - AMBIO, 10117 Berlin, Germany.
Annette SchürmannDeutsches Institut für Ernährungsforschung, Potsdam Rehbrücke, and German Center for Diabetes Research (DZD), München-Neuherberg, 14558 Potsdam-Rehbrücke, Germany.
Michael KraussLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) Berlin, Molecular Pharmacology and Cell Biology, 13125 Berlin, Germany krauss@fmp-berlin.de.ORCID 0000-0003-1010-9723
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DEDeutsches Diabetes-Zentrum e.V. · DECharité - Universitätsmedizin Berlin · DEMax Delbrück Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Compartmentalization of membrane transport and signaling processes is of pivotal importance to eukaryotic cell function. While plasma membrane compartmentalization and dynamics are well known to depend on the scaffolding function of septin GTPases, the roles of septins at intracellular membranes have remained largely elusive. Here, we show that the structural and functional integrity of the Golgi depends on its association with a septin 1 (SEPT1)-based scaffold, which promotes local microtubule nucleation and positioning of the Golgi. SEPT1 function depends on the Golgi matrix protein GM130 (also known as GOLGA2) and on centrosomal proteins, including CEP170 and components of γ-tubulin ring complex (γ-Turc), to facilitate the perinuclear concentration of Golgi membranes. Accordingly, SEPT1 depletion triggers a massive fragmentation of the Golgi ribbon, thereby compromising anterograde membrane traffic at the level of the Golgi.

Indexed as

3T3-L1 CellsAnimalsAutoantigensBiological TransportCell CompartmentationCell LineCentrosomeEpithelial CellsGene Expression RegulationGolgi ApparatusHEK293 CellsHeLa CellsHumansJurkat CellsMembrane ProteinsMiceAutoantigensCep170 protein, humanGolgin subfamily A member 2Membrane ProteinsMicrotubule-Associated ProteinsRNA, Small InterferingSEPTIN1 protein, humanSeptinsCEP170GM130GolgiMicrotubule nucleationSEPT1Septin

Identifiers

PMID30709970
PMCPMC6382012
OpenAlexW2914501813

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.