Evidence map›Paper›PMID 41296734›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

ATG2 is a triglyceride transfer protein.

Justin L Korfhage, Helin Elhan, Neng Wan, Yingying Lu, Lisa Kauffmann, Govindaiah Pilli, Devin M Fuller, Anna M Rios, Karin M Reinisch, Krishna Rao Maddipati and 2 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. ATG2 is a triglyceride transfer protein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Justin L KorfhageDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.ORCID 0000-0002-8735-982X
Helin Elhan *Laboratoire de Physique de l'École Normale Supérieure, École Normale Supérieure, Université Paris Sciences et Lettres, CNRS, Sorbonne Université, Université Paris Cité, Paris 75005, France.ORCID 0000-0002-8820-597X
Neng Wan *Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.ORCID 0000-0001-6094-2305
Yingying Lu *Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
Lisa KauffmannLaboratoire de Physique de l'École Normale Supérieure, École Normale Supérieure, Université Paris Sciences et Lettres, CNRS, Sorbonne Université, Université Paris Cité, Paris 75005, France.
Govindaiah PilliDepartment of Pathology, Lipidomics Core Facility, Wayne State University, Detroit, MI 48202.ORCID 0000-0002-0429-454X
Devin M FullerDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.ORCID 0000-0002-3049-7914
Anna M RiosDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
Karin M ReinischDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.ORCID 0000-0001-9140-6150
Krishna Rao MaddipatiDepartment of Pathology, Lipidomics Core Facility, Wayne State University, Detroit, MI 48202.ORCID 0000-0003-1445-791X
Abdou Rachid ThiamLaboratoire de Physique de l'École Normale Supérieure, École Normale Supérieure, Université Paris Sciences et Lettres, CNRS, Sorbonne Université, Université Paris Cité, Paris 75005, France.
Thomas J MeliaDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.ORCID 0000-0002-5798-4624

Funding

Molecular Basis for Membrane Lipid HomeostasisR35GM131715 · NIGMS · YALE UNIVERSITY · PI KARIN M REINISCH · 2019 to 2026
$6.5M
Mechanisms of autophagosome biogenesisR35GM153482 · NIGMS · YALE UNIVERSITY · PI Thomas James Melia · 2024 to 2026
$1.9M
Lipid flux during autophagosome membrane biogenesisR01GM135290 · NIGMS · YALE UNIVERSITY · PI MELIA, THOMAS JAMES · 2020 to 2023
$1.3M
Linear Ion Trap - Quadrupole LC-MS SystemS10OD032292 · OD · WAYNE STATE UNIVERSITY · PI MADDIPATI, KRISHNARAO · 2022 to 2022
$592k
Triple Quadrupole - Ion Trap Hybrid LC/MS/MS SystemS10RR027926 · NCRR · WAYNE STATE UNIVERSITY · PI MADDIPATI, KRISHNARAO · 2010 to 2010
$425k
ATG2 mediated lipid transport is essential for lipid droplet homeostasisF31DK136246 · NIDDK · YALE UNIVERSITY · PI KORFHAGE, JUSTIN · 2023 to 2025
$146k
ATG2 transfers lipids from ER exit site membranes to directly expand the growing autophagosomeF31AG079606 · NIA · YALE UNIVERSITY · PI FULLER, DEVIN · 2022 to 2024
$143k
Agence Nationale de la Recherche (ANR) ANR-16-TERC-0002-01Fondation pour la Recherche Médicale (FRM) EQU202103012564HHS | NIH | National Center for Research Resources (NCRR) S10RR027926HHS | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) F31DK136246HHS | NIH | National Institute of General Medical Sciences (NIGMS) GM131715HHS | NIH | National Institute of General Medical Sciences (NIGMS) GM135290HHS | NIH | National Institute of General Medical Sciences (NIGMS) GM153482HHS | NIH | National Institute on Aging (NIA) F31AG079606HHS | NIH | NIH Office of the Director (OD) S10OD032292NCRR NIH HHS S10 RR027926NIA NIH HHS F31 AG079606NIDDK NIH HHS F31 DK136246NIGMS NIH HHS R01 GM135290NIGMS NIH HHS R35 GM131715NIGMS NIH HHS R35 GM153482NIH HHS S10 OD032292Programme Emergence de la Ville de Paris DDEEES 165
6 · The paper itself

Abstract

Bridge-like lipid transfer proteins (BLTPs) are established to function in phospholipid transport between bilayers at organelle-organelle contact sites. However, the BLTP ATG2A also associates with lipid droplets in cells, which present a unique phospholipid monolayer topology and which are composed of many additional types of lipids. Whether BLTPs are active in this environment and which lipid species are substrates for transport has been unknown. Here, we use synthetic organelles with bilayers (liposomes), monolayers (artificial lipid droplets), or a mixture of the two membrane structures to demonstrate the tight binding of ATG2 specifically to monolayers via its collection of COOH-terminal amphipathic helices. This stable binding enables ATG2 to transfer phospholipids much more effectively. Unexpectedly, the neutral lipid triacylglycerol is also rapidly transported, with kinetics similar to those of phospholipid transport. Lipidomics of purified ATG2A suggests that a similar transfer of both phospholipids and triacylglycerol occurs in cells. Our work implies that BLTPs likely collect on LDs as part of a broad lipid homeostasis program, which will include the movement of both phospholipids and neutral lipids.

Indexed as

Autophagy-Related ProteinsCarrier ProteinsSaccharomyces cerevisiae ProteinsTriglyceridesBiological TransportHumansLipid DropletsLiposomesPhospholipidsSaccharomyces cerevisiaeATG2 protein, S cerevisiaeAutophagy-Related ProteinsCarrier ProteinsLiposomesPhospholipidsSaccharomyces cerevisiae ProteinsTriglyceridesATG2Abridge-like lipid transferlipid droplet

Identifiers

PMID41296734
PMCPMC12685032

What OpenQuestion holds

Textmetadata
LicenceTDM
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.