Evidence map›Paper›PMID 39485275›Full record

ArticleThe Journal of cell biology2025

Heterogeneity of late endosome/lysosomes shown by multiplexed DNA-PAINT imaging.

Charles Bond, Siewert Hugelier, Jiazheng Xing, Elena M Sorokina, Melike Lakadamyali

Abstract read
In one paragraph

Article in The Journal of cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Article
  2. Supramolecular Degraders: An Emerging Paradigm in Targeted Protein Degradation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Active transport of tRNAs facilitates distributed protein synthesis.bioRxiv : the preprint server for biology · 2026
    Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Charles BondDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0003-1395-0112
Siewert HugelierDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0002-6224-652X
Jiazheng XingDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0009-0001-4587-126X
Elena M SorokinaDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0003-2079-869X
Melike LakadamyaliDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0002-7524-6414

Funding

Integrative mechanisms of organelle dynamics from the atomic-to-cellular levelRM1GM136511 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO, HOLZBAUR, ERIKA L · 2020 to 2024
$7.4M
Quantitative super-resolution imaging to map the multi-scale functional organization of cellsR35GM152111 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Melike Lakadamyali · 2024 to 2026
$1.7M
Calibration nanotemplates as universal standards for determining protein copy number in super-resolution microscopyR01GM133842 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LAKADAMYALI, MELIKE · 2019 to 2022
$1.7M
National Science Foundation CMMI-1548571NIGMS NIH HHS R01 GM133842NIGMS NIH HHS R35 GM152111NIGMS NIH HHS RM1 GM136511NIH HHS R01 GM133842
6 · The paper itself

Abstract

Late endosomes/lysosomes (LELs) are crucial for numerous physiological processes and their dysfunction is linked to many diseases. Proteomic analyses have identified hundreds of LEL proteins; however, whether these proteins are uniformly present on each LEL, or if there are cell-type-dependent LEL subpopulations with unique protein compositions is unclear. We employed quantitative, multiplexed DNA-PAINT super-resolution imaging to examine the distribution of seven key LEL proteins (LAMP1, LAMP2, CD63, Cathepsin D, TMEM192, NPC1, and LAMTOR4). While LAMP1, LAMP2, and Cathepsin D were abundant across LELs, marking a common population, most analyzed proteins were associated with specific LEL subpopulations. Our multiplexed imaging approach identified up to eight different LEL subpopulations based on their unique membrane protein composition. Additionally, our analysis of the spatial relationships between these subpopulations and mitochondria revealed a cell-type-specific tendency for NPC1-positive LELs to be closely positioned to mitochondria. Our approach will be broadly applicable to determining organelle heterogeneity with single organelle resolution in many biological contexts.

Indexed as

EndosomesLysosomesCathepsin DDNAHumansLysosomal-Associated Membrane Protein 1Lysosomal-Associated Membrane Protein 2Lysosomal Membrane ProteinsMitochondriaNiemann-Pick C1 ProteinTetraspanin 30Cathepsin DCD63 protein, humanDNALAMP1 protein, humanLAMP2 protein, humanLysosomal-Associated Membrane Protein 1Lysosomal-Associated Membrane Protein 2Lysosomal Membrane ProteinsNiemann-Pick C1 ProteinNPC1 protein, humanTetraspanin 30

Identifiers

PMID39485275
PMCPMC11533445

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.