Evidence map›Paper›PMID 26490117›Full record

ArticleMolecular biology of the cell2015

CARTS biogenesis requires VAP-lipid transfer protein complexes functioning at the endoplasmic reticulum-Golgi interface.

Yuichi Wakana, Richika Kotake, Nanako Oyama, Motohide Murate, Toshihide Kobayashi, Kohei Arasaki, Hiroki Inoue, Mitsuo Tagaya

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023
    Review
  9. Review
  10. Sending out molecules from the TGN.Current opinion in cell biology · 2021
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. The Fast and the Furious: Golgi Contact Sites.Contact (Thousand Oaks (Ventura County, Calif.)) · 2021
    Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article
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

8 authors at 2 institutions in 1 country.

Yuichi WakanaSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan.
Richika KotakeSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan.
Nanako OyamaSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan.
Motohide MurateLipid Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan.
Toshihide KobayashiLipid Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan.
Kohei ArasakiSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan.
Hiroki InoueSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan.
Mitsuo TagayaSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan tagaya@toyaku.ac.jp.
Tokyo University of Pharmacy and Life Sciences · JPRIKEN · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vesicle-associated membrane protein-associated protein (VAP) is an endoplasmic reticulum (ER)-resident integral membrane protein that controls a nonvesicular mode of ceramide and cholesterol transfer from the ER to the Golgi complex by interacting with ceramide transfer protein and oxysterol-binding protein (OSBP), respectively. We report that VAP and its interacting proteins are required for the processing and secretion of pancreatic adenocarcinoma up-regulated factor, whose transport from the trans-Golgi network (TGN) to the cell surface is mediated by transport carriers called "carriers of the trans-Golgi network to the cell surface" (CARTS). In VAP-depleted cells, diacylglycerol level at the TGN was decreased and CARTS formation was impaired. We found that VAP forms a complex with not only OSBP but also Sac1 phosphoinositide phosphatase at specialized ER subdomains that are closely apposed to the trans-Golgi/TGN, most likely reflecting membrane contact sites. Immobilization of ER-Golgi contacts dramatically reduced CARTS production, indicating that association-dissociation dynamics of the two membranes are important. On the basis of these findings, we propose that the ER-Golgi contacts play a pivotal role in lipid metabolism to control the biogenesis of transport carriers from the TGN.

Indexed as

CeramidesCholesterolEndoplasmic ReticulumHEK293 CellsHumansIntercellular Signaling Peptides and ProteinsLectinsMembrane FusionProtein Kinase CProtein Serine-Threonine KinasesR-SNARE Proteinstrans-Golgi NetworkVesicular Transport ProteinsCeramidesCERT1 protein, humanCholesterolIntercellular Signaling Peptides and ProteinsLectinsProtein Kinase Cprotein kinase DProtein Serine-Threonine KinasesR-SNARE ProteinsVAPA protein, humanVesicular Transport ProteinsZG16B protein, human

Identifiers

PMID26490117
PMCPMC4678024
OpenAlexW2179080294

What OpenQuestion holds

Textmetadata
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.