Evidence map›Paper›PMID 28003315›Full record

ArticleThe EMBO journal2017

COPI-TRAPPII activates Rab18 and regulates its lipid droplet association.

Chunman Li, Xiaomin Luo, Shan Zhao, Gavin Ky Siu, Yongheng Liang, Hsiao Chang Chan, Ayano Satoh, Sidney Sb Yu

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
8.7field-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

60 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Diatom triacylglycerol metabolism: from carbon fixation to lipid droplet degradation.Biological reviews of the Cambridge Philosophical Society · 2025
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  5. Molecular therapy. Nucleic acids · 2024
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  12. Article
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  14. The evolving landscape of ER-LD contact sites.Frontiers in cell and developmental biology · 2024
    Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. The role of CaMKK2 in Golgi-associated vesicle trafficking.Biochemical Society transactions · 2023
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Chunman LiDepartment of Anatomy, Histology and Developmental Biology, School of Basic Medical Sciences, Health Science Centre, Shenzhen University, Shenzhen, China.ORCID 0000-0003-1674-7136
Xiaomin LuoSchool of Biomedical Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China.
Shan ZhaoSchool of Biomedical Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China.
Gavin Ky SiuSchool of Biomedical Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China.
Yongheng LiangKey Laboratory of Agricultural Environmental Microbiology of MOA, College of Life Sciences, Nanjing Agricultural University, Nanjing, China.
Hsiao Chang ChanSchool of Biomedical Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China.
Ayano SatohThe Graduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
Sidney Sb YuSchool of Biomedical Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China sidney.yu@cuhk.edu.hk.ORCID 0000-0001-9643-2729
Chinese University of Hong Kong · HKNanjing Agricultural University · CNOkayama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transport protein particle (TRAPP) was initially identified as a vesicle tethering factor in yeast and as a guanine nucleotide exchange factor (GEF) for Ypt1/Rab1. In mammals, structures and functions of various TRAPP complexes are beginning to be understood. We found that mammalian TRAPPII was a GEF for both Rab18 and Rab1. Inactivation of TRAPPII-specific subunits by various methods including siRNA depletion and CRISPR-Cas9-mediated deletion reduced lipolysis and resulted in aberrantly large lipid droplets. Recruitment of Rab18 onto lipid droplet (LD) surface was defective in TRAPPII-deleted cells, but the localization of Rab1 on Golgi was not affected. COPI regulates LD homeostasis. We found that the previously documented interaction between TRAPPII and COPI was also required for the recruitment of Rab18 to the LD We hypothesize that the interaction between COPI and TRAPPII helps bring TRAPPII onto LD surface, and TRAPPII, in turn, activates Rab18 and recruits it on the LD surface to facilitate its functions in LD homeostasis.

Indexed as

Cell LineCoat Protein Complex IGene Knockdown TechniquesGene Knockout TechniquesHumansLipid DropletsLipolysisrab1 GTP-Binding Proteinsrab GTP-Binding ProteinsVesicular Transport ProteinsCoat Protein Complex IRAB18 protein, humanrab1 GTP-Binding Proteinsrab GTP-Binding Proteinstransport protein particle, TRAPPVesicular Transport ProteinsCOPIlipid dropletsRab18TRAPPC10TRAPPC9TRAPPII

Identifiers

PMID28003315
PMCPMC5694949
OpenAlexW2564664285

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.