Evidence map›Paper›PMID 27879284›Full record

ArticleThe EMBO journal2016

Seipin regulates ER-lipid droplet contacts and cargo delivery.

Veijo T Salo, Ilya Belevich, Shiqian Li, Leena Karhinen, Helena Vihinen, Corinne Vigouroux, Jocelyne Magré, Christoph Thiele, Maarit Hölttä-Vuori, Eija Jokitalo and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 187 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
187citing papers in PubMed, 1 pooled it
23.9field-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

187 citing papers in PubMed, 1 synthesis or guideline pooled it, 316 citations in OpenAlex.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
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127 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

11 authors at 3 institutions in 2 countries.

Veijo T SaloDepartment of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
Ilya BelevichInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.
Shiqian LiDepartment of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-1663-0704
Leena KarhinenDepartment of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
Helena VihinenInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.
Corinne VigourouxSorbonne Universités, UPMC Univ Paris 6, Inserm UMR_S938, Saint-Antoine Research Center, Institute of Cardiometabolism And Nutrition, AP-HP, Saint-Antoine Hospital Department of Molecular Biology and Genetics, Paris, France.
Jocelyne Magrél'Institut du Thorax, INSERM CNRS UNIV Nantes, Nantes, France.
Christoph ThieleLIMES Institute, Bonn University, Bonn, Germany.
Maarit Hölttä-VuoriDepartment of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
Eija JokitaloInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.
Elina IkonenDepartment of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland elina.ikonen@helsinki.fi.
University of Helsinki · FICentre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Seipin is an endoplasmic reticulum (ER) membrane protein implicated in lipid droplet (LD) biogenesis and mutated in severe congenital lipodystrophy (BSCL2). Here, we show that seipin is stably associated with nascent ER-LD contacts in human cells, typically via one mobile focal point per LD Seipin appears critical for such contacts since ER-LD contacts were completely missing or morphologically aberrant in seipin knockout and BSCL2 patient cells. In parallel, LD mobility was increased and protein delivery from the ER to LDs to promote LD growth was decreased. Moreover, while growing LDs normally acquire lipid and protein constituents from the ER, this process was compromised in seipin-deficient cells. In the absence of seipin, the initial synthesis of neutral lipids from exogenous fatty acid was normal, but fatty acid incorporation into neutral lipids in cells with pre-existing LDs was impaired. Together, our data suggest that seipin helps to connect newly formed LDs to the ER and that by stabilizing ER-LD contacts seipin facilitates the incorporation of protein and lipid cargo into growing LDs in human cells.

Indexed as

Cells, CulturedEndoplasmic ReticulumGene Knockout TechniquesGTP-Binding Protein gamma SubunitsHumansLipid DropletsModels, BiologicalBSCL2 protein, humanGTP-Binding Protein gamma Subunitselectron microscopylipid storagelipodystrophymembrane contact sites

Identifiers

PMID27879284
PMCPMC5167346
OpenAlexW2552567900

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.