Evidence map›Paper›PMID 36266287›Full record

ArticleNature communications2022

Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo.

Jasjot Singh, Hadeer Elhabashy, Pathma Muthukottiappan, Markus Stepath, Martin Eisenacher, Oliver Kohlbacher, Volkmar Gieselmann, Dominic Winter

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
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  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Revealing the architecture of the membrane-bound Flotillin cage assembly.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Structure of the flotillin complex in a native membrane environment.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Review
  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 4 institutions in 1 country.

Jasjot SinghInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, 53115, Bonn, Germany.ORCID 0000-0002-9203-2047
Hadeer ElhabashyDepartment of Protein Evolution, Max-Planck-Institute for Developmental Biology, 72076, Tübingen, Germany.ORCID 0000-0002-4677-7064
Pathma MuthukottiappanInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, 53115, Bonn, Germany.ORCID 0000-0003-2812-2723
Markus StepathMedical Proteome-Center, Medical Faculty, Ruhr-University Bochum, 48801, Bochum, Germany.
Martin EisenacherMedical Proteome-Center, Medical Faculty, Ruhr-University Bochum, 48801, Bochum, Germany.ORCID 0000-0003-2687-7444
Oliver KohlbacherInstitute for Bioinformatics and Medical Informatics, University of Tübingen, 72076, Tübingen, Germany.ORCID 0000-0003-1739-4598
Volkmar GieselmannInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, 53115, Bonn, Germany.ORCID 0000-0001-9410-4617
Dominic WinterInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, 53115, Bonn, Germany. dominic.winter@uni-bonn.de.ORCID 0000-0001-6788-6641
University of Bonn · DERuhr University Bochum · DEBernstein Center for Computational Neuroscience Tübingen · DEMax Planck Institute for Developmental Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysosomes are well-established as the main cellular organelles for the degradation of macromolecules and emerging as regulatory centers of metabolism. They are of crucial importance for cellular homeostasis, which is exemplified by a plethora of disorders related to alterations in lysosomal function. In this context, protein complexes play a decisive role, regulating not only metabolic lysosomal processes but also lysosome biogenesis, transport, and interaction with other organelles. Using cross-linking mass spectrometry, we analyze lysosomes and early endosomes. Based on the identification of 5376 cross-links, we investigate protein-protein interactions and structures of lysosome- and endosome-related proteins. In particular, we present evidence for a tetrameric assembly of the lysosomal hydrolase PPT1 and a heterodimeric structure of FLOT1/FLOT2 at lysosomes and early endosomes. For FLOT1-/FLOT2-positive early endosomes, we identify >300 putative cargo proteins and confirm eleven substrates for flotillin-dependent endocytosis, including the latrophilin family of adhesion G protein-coupled receptors.

Indexed as

EndosomesLysosomesHydrolasesMembrane ProteinsflotillinsHydrolasesMembrane Proteins

Identifiers

PMID36266287
PMCPMC9584938
OpenAlexW4306861808

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.