Evidence map›Paper›PMID 31636202›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes.

Andrés Guillén-Samander, Xin Bian, Pietro De Camilli

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed, 1 pooled it
5.6field-weighted citation impact, top 3% 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

51 citing papers in PubMed, 1 synthesis or guideline pooled it, 86 citations in OpenAlex.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  2. Article
  3. Article
  4. LYVAC/PDZD8 is a lysosomal vacuolator.Science (New York, N.Y.) · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Lysosomes' fallback strategies: more than just survival or death.Frontiers in cell and developmental biology · 2025
    Review
  9. Article
  10. Article
  11. The p53 target DRAM1 modulates calcium homeostasis and ER stress by promoting contact between lysosomes and the ER through STIM1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Lysosomal Ion Channels and Lysosome-Organelle Interactions.Handbook of experimental pharmacology · 2023
    Article
  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

3 authors at 1 institution in 1 country.

Andrés Guillén-SamanderHHMI, Yale University School of Medicine, New Haven, CT 06510.
Xin BianHHMI, Yale University School of Medicine, New Haven, CT 06510.
Pietro De CamilliHHMI, Yale University School of Medicine, New Haven, CT 06510; Pietro.decamilli@yale.edu.
Yale University · US

Funding

Yale Diabetes Research CenterP30DK045735 · NIDDK · YALE UNIVERSITY · PI Richard A Flavell · 1993 to 2026
$44.0M
Yale/NIDA Neuroproteomics Research CenterP30DA018343 · NIDA · YALE UNIVERSITY · PI Marina R Picciotto · 2004 to 2026
$37.1M
MOLECULAR MECHANISMS IN SYNAPTIC VESICLE RECYCLINGR01NS036251 · NINDS · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 1997 to 2021
$4.7M
Molecular Mechanisms in Synaptic Vesicle RecyclingR37NS036251 · NINDS · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 2010 to 2016
$2.7M
NIDA NIH HHS P30 DA018343NIDDK NIH HHS P30 DK045735NINDS NIH HHS R01 NS036251NINDS NIH HHS R37 NS036251
6 · The paper itself

Abstract

Contacts between the endoplasmic reticulum (ER) and other membranes are hot spots for protein-mediated lipid transport between the 2 adjacent bilayers. Compiling a molecular inventory of lipid transport proteins present at these sites is a premise to the elucidation of their function. Here we show that PDZD8, an intrinsic membrane protein of the ER with a lipid transport module of the SMP domain family, concentrates at contacts between the ER and late endosomes/lysosomes, where it interacts with GTP-Rab7. These findings suggest that PDZD8 may cooperate with other proteins that function at the ER-endo/lysosome interface in coordinating endocytic flow with lipid transport between endocytic membranes and the ER.

Indexed as

Adaptor Proteins, Signal TransducingCell MembraneEndoplasmic ReticulumEndosomesHumansLysosomesProtein BindingProtein DomainsProtein Transportrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsAdaptor Proteins, Signal TransducingPDZD8 protein, humanrab7 GTP-Binding Proteinsrab7 GTP-binding proteins, humanrab GTP-Binding Proteinslipid-transfer proteinmembrane contact sitesSMP domain

Identifiers

PMID31636202
PMCPMC6842579
OpenAlexW2981916477

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.