Evidence map›Paper›PMID 41496216›Full record

ArticleRedox biology2026

A clickable CoQ imaging probe reveals that cellular uptake and lysosomal trafficking depend on CD36 and NPC1.

Irene Liparulo, Arkadiy Bazhin, Grace Katherine Van Wyhe, Amanda Lestari Gunawan, Neville Dadina, Justin Hyunwoo Kwon, Alanna Schepartz, Elena Goun, Andreas Stahl

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Redox biology, 2026. 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
–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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Irene LiparuloDepartment of Nutritional Sciences and Toxicology, University of California, Berkeley, CA, 94720, USA.
Arkadiy BazhinDepartment of Chemistry, University of Missouri, Columbia, MO, 65211, USA.
Grace Katherine Van WyheDepartment of Nutritional Sciences and Toxicology, University of California, Berkeley, CA, 94720, USA.
Amanda Lestari GunawanDepartment of Nutritional Sciences and Toxicology, University of California, Berkeley, CA, 94720, USA.
Neville DadinaDepartment of Chemistry, University of California, Berkeley, CA, 94720, USA.
Justin Hyunwoo KwonDepartment of Chemistry, University of California, Berkeley, CA, 94720, USA.
Alanna SchepartzDepartment of Chemistry, University of California, Berkeley, CA, 94720, USA.
Elena GounDepartment of Chemistry, University of Missouri, Columbia, MO, 65211, USA. Electronic address: elena.goun@missouri.edu.
Andreas StahlDepartment of Nutritional Sciences and Toxicology, University of California, Berkeley, CA, 94720, USA. Electronic address: astahl@berkeley.edu.

Funding

Fluorescence tools that illuminate biology and inspire translationR35GM134963 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI Alanna Schepartz · 2020 to 2026
$4.7M
Role of CoQ in regulating thermogenesisR01DK126830 · NIDDK · UNIVERSITY OF CALIFORNIA BERKELEY · PI STAHL, ANDREAS · 2021 to 2024
$1.8M
Optical platform for functional longitudinal imaging of metabolite uptake in vivoR01EB034607 · NIBIB · UNIVERSITY OF MISSOURI-COLUMBIA · PI Elena Goun · 2023 to 2026
$1.5M
NIBIB NIH HHS 3R01EB034607-01A1S1NIBIB NIH HHS R01 EB034607NIDDK NIH HHS R01 DK126830NIGMS NIH HHS R35 GM134963
6 · The paper itself

Abstract

Coenzyme Q (CoQ) is a crucial lipid-soluble antioxidant and electron transporter vital for mitochondrial respiration and cellular redox balance. Despite the role of CoQ in oxidative phosphorylation being well established, the mechanisms by which CoQ is internalized, distributed among subcellular compartments, and trafficked to mitochondria remain poorly defined. Here, we present the development of a minimally modified, azide-tagged CoQ analogue that enables high-resolution visualization of CoQ localization using fluorescence-based imaging. Using this probe, we focus our investigation on brown adipose tissue (BAT), a mitochondria-rich, highly metabolically active tissue with elevated CoQ demand. On a cellular level, we demonstrate that CoQ is internalized via receptor-mediated endocytosis, predominantly localizing to lysosomes. Genetic knockdown and pharmacological studies identify CD36 and NPC1 as essential transporters in this process. Our work provides both a technical advance for the redox biology field, with the development and characterization of a CoQ probe, and the essential new biological insight that NPC1 is linked to CoQ homeostasis and thus provides a foundation for further dissection of CoQ biology in health and disease.

Indexed as

Carrier ProteinsCD36 AntigensLysosomesUbiquinoneAnimalsClick ChemistryEndocytosisHumansIntracellular Signaling Peptides and ProteinsMitochondriaNiemann-Pick C1 ProteinProtein TransportCarrier ProteinsCD36 AntigensIntracellular Signaling Peptides and ProteinsNiemann-Pick C1 ProteinNPC1 protein, humanUbiquinone

Identifiers

PMID41496216
PMCPMC12808830

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.