Evidence map›Paper›PMID 29806001›Full record

ArticleACS central science2018

A Ceramide-Regulated Element in the Late Endosomal Protein LAPTM4B Controls Amino Acid Transporter Interaction.

Kecheng Zhou, Andrea Dichlberger, Hector Martinez-Seara, Thomas K M Nyholm, Shiqian Li, Young Ah Kim, Ilpo Vattulainen, Elina Ikonen, Tomas Blom

Open access · diamondAbstract read
In one paragraph

Article in ACS central science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

29 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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 4 institutions in 3 countries.

Kecheng ZhouDepartment of Anatomy, Faculty of Medicine, University of Helsinki, 00014 Helsinki, Finland.
Andrea DichlbergerDepartment of Anatomy, Faculty of Medicine, University of Helsinki, 00014 Helsinki, Finland.
Hector Martinez-SearaInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Academy of Sciences of the Czech Republic, 166 10 Prague, Czech Republic.
Thomas K M NyholmBiochemistry, Faculty of Science and Engineering, Åbo Akademi University, 20520 Turku, Finland.
Shiqian LiDepartment of Anatomy, Faculty of Medicine, University of Helsinki, 00014 Helsinki, Finland.
Young Ah KimDepartment of Chemistry and Biochemistry, Queens College, City University of New York, Flushing, New York 11367, United States.
Ilpo VattulainenLaboratory of Physics, Tampere University of Technology, 33101 Tampere, Finland.
Elina IkonenDepartment of Anatomy, Faculty of Medicine, University of Helsinki, 00014 Helsinki, Finland.
Tomas BlomDepartment of Anatomy, Faculty of Medicine, University of Helsinki, 00014 Helsinki, Finland.
University of Helsinki · FIÅbo Akademi University · FIQueens College, CUNY · USTampere University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane proteins are functionally regulated by the composition of the surrounding lipid bilayer. The late endosomal compartment is a central site for the generation of ceramide, a bioactive sphingolipid, which regulates responses to cell stress. The molecular interactions between ceramide and late endosomal transmembrane proteins are unknown. Here, we uncover in atomistic detail the ceramide interaction of Lysosome Associated Protein Transmembrane 4B (LAPTM4B), implicated in ceramide-dependent cell death and autophagy, and its functional relevance in lysosomal nutrient signaling. The ceramide-mediated regulation of LAPTM4B depends on a sphingolipid interaction motif and an adjacent aspartate residue in the protein's third transmembrane (TM3) helix. The interaction motif provides the preferred contact points for ceramide while the neighboring membrane-embedded acidic residue confers flexibility that is subject to ceramide-induced conformational changes, reducing TM3 bending. This facilitates the interaction between LAPTM4B and the amino acid transporter heavy chain 4F2hc, thereby controlling mTORC signaling. These findings provide mechanistic insights into how transmembrane proteins sense and respond to ceramide.

Identifiers

PMID29806001
PMCPMC5968438
OpenAlexW2800545681

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.