Evidence map›Paper›PMID 41065314›Full record

ArticleJournal of cell science2025

Dynamics of Fanconi anemia protein D2 in association with nuclear lipid droplet formation.

Tomoya Hotani, Motonari Goto, Yukie Otsuki, Shun Matsuda, Nobuhiro Wada, Masakazu Shinohara, Tomonari Matsuda, Masayuki Yokoi, Kaoru Sugasawa, Yuki Ohsaki and 1 more

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In one paragraph

Article in Journal of cell science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

11 authors.

Tomoya HotaniBiosignal Research Center, Kobe University, Kobe 657-8501, Japan.
Motonari GotoBiosignal Research Center, Kobe University, Kobe 657-8501, Japan.
Yukie OtsukiBiosignal Research Center, Kobe University, Kobe 657-8501, Japan.
Shun MatsudaResearch Center for Environmental Quality Management, Graduate School of Engineering, Kyoto University, Otsu 520-0811, Japan.
Nobuhiro WadaDivision of Cell and Tissue Morphology, Department of Anatomy, School of Medicine, Sapporo Medical University, Sapporo 060-8556, Japan.
Masakazu ShinoharaDivision of Molecular Epidemiology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.
Tomonari MatsudaResearch Center for Environmental Quality Management, Graduate School of Engineering, Kyoto University, Otsu 520-0811, Japan.
Masayuki YokoiBiosignal Research Center, Kobe University, Kobe 657-8501, Japan.ORCID 0000-0001-9727-0258
Kaoru SugasawaBiosignal Research Center, Kobe University, Kobe 657-8501, Japan.ORCID 0000-0001-7937-4053
Yuki OhsakiDivision of Cell and Tissue Morphology, Department of Anatomy, School of Medicine, Sapporo Medical University, Sapporo 060-8556, Japan.
Wataru SakaiBiosignal Research Center, Kobe University, Kobe 657-8501, Japan.ORCID 0000-0002-6561-5773

Funding

Japan Science and Technology AgencyJapan Society for the Promotion of Science 17K07286Japan Society for the Promotion of Science 20K06487Japan Society for the Promotion of Science 21K06733Japan Society for the Promotion of Science 24K02208Japan Society for the Promotion of Science London 17K07286Japan Society for the Promotion of Science London 20K06487Japan Society for the Promotion of Science London 21K06733Japan Society for the Promotion of Science London 24K02208Takeda Science Foundation
6 · The paper itself

Abstract

Fanconi anemia is a rare genetic disease caused by the loss of function of one of the 23 associated genes and is characterized by bone marrow failure, cancer predisposition and developmental defects. The proteins encoded by these genes (FANC proteins) mainly function in DNA damage response and repair. Although FANC deficiency has multiple effects on the regulation of lipid metabolism, the molecular function of FANC proteins in the context of Fanconi anemia pathology remains unclear. In the present study, we demonstrate that FANCD2, a key component of FANC proteins, interacts with factors involved in fatty acid biosynthesis or sphingolipid metabolism and that FANCD2 deficiency downregulates the cellular levels of fatty acids. Moreover, a portion of FANCD2 is localized to nuclear lipid droplets in response to oleic acid (OA) treatment. These subcellular dynamics are independent of FANCD2 monoubiquitylation, which is essential for the DNA damage response. Collectively, these findings demonstrate that FANCD2 responds to not only DNA damage but also OA exposure, providing insights into the pathogenesis of lipid dysregulation in Fanconi anemia.

Indexed as

Cell NucleusFanconi Anemia Complementation Group D2 ProteinLipid DropletsAnimalsDNA DamageFanconi AnemiaHumansFANCD2 protein, humanFanconi Anemia Complementation Group D2 ProteinDNA damage responseFanconi anemiaLipid dropletLipid metabolism

Identifiers

PMID41065314
PMCPMC12669972

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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.