Evidence map›Paper›PMID 29750412›Full record

ArticleJournal of molecular cell biology2019

ACBD3 is required for FAPP2 transferring glucosylceramide through maintaining the Golgi integrity.

Jing Liao, Yuxiang Guan, Wei Chen, Can Shi, Dongdong Yao, Fengsong Wang, Sin Man Lam, Guanghou Shui, Xinwang Cao

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Infection and immunity · 2026
    Article
  2. Context-dependent Interactors Regulate TDP-43 Dysfunction in ALS/FTLD.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Sphingolipid metabolism and regulated cell death in malignant melanoma.Apoptosis : an international journal on programmed cell death · 2024
    Review
  5. Article
  6. Article
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  9. Article
  10. Review
  11. Article
  12. Gangliosides and Neuroblastomas.International journal of molecular sciences · 2020
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Acylation - A New Means to Control Traffic Through the Golgi.Frontiers in cell and developmental biology · 2019
    Review
  20. 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

9 authors at 3 institutions in 1 country.

Jing LiaoSchool of Life Sciences, Anhui Medical University, Hefei, China.
Yuxiang GuanSchool of Life Sciences, Anhui Medical University, Hefei, China.
Wei ChenSchool of Life Sciences, Anhui Medical University, Hefei, China.
Can ShiSchool of Life Sciences, Anhui Medical University, Hefei, China.
Dongdong YaoSchool of Life Sciences, Anhui Medical University, Hefei, China.
Fengsong WangSchool of Life Sciences, Anhui Medical University, Hefei, China.
Sin Man LamState Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Guanghou ShuiState Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Xinwang CaoSchool of Life Sciences, Anhui Medical University, Hefei, China.
Anhui Medical University · CNChinese Academy of Sciences · CNInstitute of Genetics and Developmental Biology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosphingolipid (GSL) metabolism is involved in various physiological processes, including all major cell signaling pathways, and its dysregulation is linked to some diseases. The four-phosphate adaptor protein FAPP2-mediated glucosylceramide (GlcCer) transport for complex GSL synthesis has been studied extensively. However, the molecular machinery of FAPP2 as a GlcCer-transferring protein remains poorly defined. Here, we identify a Golgi-resident protein, acyl-coenzyme A binding domain containing 3 (ACBD3), as an interacting partner of FAPP2. We find that ACBD3 knockdown leads to dramatic Golgi fragmentation, which subsequently causes FAPP2 dispersal throughout the cytoplasm and a decreased localization at trans-Golgi network. The further quantitative lipidomic analysis indicates that ACBD3 knockdown triggers abnormal sphingolipid metabolism. Interestingly, the expression of siRNA-resistant full-length ACBD3 can rescue these defects caused by ACBD3 knockdown. These data reveal critical roles for ACBD3 in maintaining the integrity of Golgi morphology and cellular sphingolipid homeostasis and establish the importance of the integrated Golgi complex for the transfer of GlcCer and complex GSL synthesis.

Indexed as

Adaptor Proteins, Signal TransducingGlucosylceramidesGlycosphingolipidsGolgi ApparatusHumansMembrane Proteinstrans-Golgi NetworkACBD3 protein, humanAdaptor Proteins, Signal TransducingGlucosylceramidesGlycosphingolipidsMembrane ProteinsPLEKHA8 protein, humanACBD3FAPP2glucosylceramideglycosphingolipidsGolgi fragmentation

Identifiers

PMID29750412
PMCPMC6734144
OpenAlexW2801698800

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.