Evidence map›Paper›PMID 41652064›Full record

ArticleNature chemical biology2026

Photosensitizer proximity labeling captures the lipid and protein interactomes.

Andrew P Becker, Elijah Biletch, John Paul Kennelly, Soon-Gook Hong, Ashley R Julio, Miranda Villanueva, Rohith T Nagari, Daniel W Turner, Nikolas R Burton, Tomoyuki Fukuta and 7 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Review
  3. AbioRxiv : the preprint server for biology · 2026
    Article
  4. A unified photosensitizer platform forbioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors.

Andrew P BeckerDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0002-1654-0912
Elijah BiletchDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0002-3723-536X
John Paul KennellyDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0002-4399-3976
Soon-Gook HongMolecular Biology Institute, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0002-1385-4430
Ashley R JulioDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0002-6258-2849
Miranda VillanuevaDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0002-4892-8356
Rohith T NagariDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.
Daniel W TurnerDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA, USA.
Nikolas R BurtonDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0003-2887-8846
Tomoyuki FukutaDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.
Liujuan CuiDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0001-6186-1558
Xu XiaoDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0002-5033-7627
Zaid VellaniDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA, USA.
Alexander NguyenVatche and Tamar Manoukian Division of Digestive Diseases, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0001-6578-3454
Julia J MackMolecular Biology Institute, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0002-9239-8436
Peter TontonozDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0003-1259-0477
Keriann M BackusDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA. kbackus@mednet.ucla.edu.ORCID http://orcid.org/0000-0001-8541-1404

Funding

UCLA-Caltech Medical Scientist Training ProgramT32GM008042 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI AJIJOLA, OLUJIMI A, DAWSON, DAVID WAYNE · 1985 to 2023
$29.9M
Chemistry Biology Interface Training ProgramT32GM136614 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Patrick G. Harran · 2020 to 2026
$2.8M
American Heart Association (American Heart Association, Inc.) 903306David and Lucile Packard Foundation (David & Lucile Packard Foundation) Packard FellowshioFondation Leducq 19CVD04NIGMS NIH HHS T32 GM008042NIGMS NIH HHS T32 GM136614U.S. Department of Health & Human Services | NIH | National Heart, Lung, and Blood Institute (NHLBI) 1P01HL146358U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) DP2 GM146246-02U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) T32 GM008042U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) T32 GM136614
6 · The paper itself

Abstract

The physical properties of cellular membranes are influenced by protein and lipid interactions. In situ proximity labeling interactomic methods are well suited to characterize these dynamic and often fleeting interactions. Yet, available methods require distinct chemistries for proteins and lipids. Here we establish a singlet oxygen-based photocatalytic proximity labeling platform (POCA) that reports intracellular interactomes for both proteins and lipids using cell-penetrant photosensitizer reagents. Cholesterol-directed POCA captured known and unprecedented cholesterol-binding proteins, including protein complexes sensitive to intracellular cholesterol levels and proteins uniquely captured by physiologically relevant lipoprotein uptake. Protein-directed POCA accurately mapped intracellular membrane complexes, defined sterol-dependent changes to the interactome of the cholesterol transport protein Aster-B and revealed singlet oxygen-mediated domain-specific Aster crosslinking. More broadly, we find that POCA is a versatile interactomics platform that is straightforward to implement, using the readily available HaloTag system, fulfilling unmet needs in intracellular singlet oxygen-based proximity labeling proteomics.

Indexed as

LipidsPhotosensitizing AgentsProteinsCholesterolHumansProtein BindingProteomicsSinglet OxygenStaining and LabelingCholesterolLipidsPhotosensitizing AgentsProteinsSinglet Oxygen

Identifiers

PMID41652064

What OpenQuestion holds

Textmetadata
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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.