Evidence map›Paper›PMID 41045928›Full record

ArticleNeuron2025

Identification of the peptide Vulnusin, a wound signal that mediates mechanical-injury-induced nociception in Drosophila.

Yanmeng Guo, Tun Li, Sami T Tuomivaara, Chin Fen Teo, Shengjie Feng, Robert J Chalkley, Ruijun Zhu, Tong Cheng, Kathy H Li, Wei Chen and 9 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Neuron, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

19 authors.

Yanmeng GuoDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Tun LiDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Sami T TuomivaaraDepartment of Obstetrics, Gynecology, and Reproductive Sciences, Center for Reproductive Sciences, Eli and Edythe Broad Center for Regeneration Medicine and Stem Cell Research, Sandler-Moore Mass Spectrometry Core Facility, University of California at San Francisco, San Francisco, CA 94143, USA.
Chin Fen TeoDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Shengjie FengDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Robert J ChalkleyMass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California at San Francisco, San Francisco, CA 94143, USA.
Ruijun ZhuDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Tong ChengDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Kathy H LiMass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California at San Francisco, San Francisco, CA 94143, USA.
Wei ChenDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Avi SimonDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Peng JinDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Susan YoungerDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Adeline J H YongDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Kai LiDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Kexin LiDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Alma L BurlingameMass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California at San Francisco, San Francisco, CA 94143, USA.
Lily Yeh JanDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA.
Yuh Nung JanDepartment of Physiology, Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94143, USA. Electronic address: yuhnung.jan@ucsf.edu.

Funding

Dendrite morphogenesis, function and regenerationR35NS097227 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JAN, YUH NUNG · 2017 to 2024
$5.1M
The TMEM16 Family of Ion Channels and Lipid ScramblasesR35NS122110 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LILY JAN · 2021 to 2026
$3.2M
Dendrite development, function, degeneration and regenerationR35NS137312 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI YUH NUNG JAN · 2025 to 2026
$1.4M
NINDS NIH HHS R35 NS097227NINDS NIH HHS R35 NS122110NINDS NIH HHS R35 NS137312
6 · The paper itself

Abstract

Animals can acutely sense a puncture or cut in their skin through nociceptors. However, the molecular identity of such "wound signals" and their receptors on nociceptors remains unknown. In Drosophila larvae, class IV dendritic arborization neurons are multimodal nociceptors that detect harsh touch, heat, and UV light to initiate nociceptive behavior. Here, we identify Vulnusin (from vulnus, a Latin word for wound), an endogenous peptide likely serving as a wound signal. Vulnusin, derived from the larval epidermis, activates PPK1/PPK26 ion channels expressed endogenously on nociceptors and heterologously in Drosophila S2 cells. Moreover, Vulnusin acts together with PPK1/PPK26 to trigger puncture-induced rolling behavior, a response to mechanical injury. These findings establish Vulnusin as a ligand that activates larval nociceptors and mediates mechanical-injury-induced nociception.

Indexed as

Drosophila ProteinsEpithelial Sodium ChannelsNociceptionSodium ChannelsWounds and InjuriesAnimalsAnimals, Genetically ModifiedCell LineDisease Models, AnimalDrosophilaEpidermisGene Knockout TechniquesLarvaNociceptorsSignal TransductionDrosophila ProteinsEpithelial Sodium ChannelsPPK26 protein, Drosophilappk protein, DrosophilaSodium Channelsinjury-induced nociceptionion channelpeptidewound signal

Identifiers

PMID41045928
PMCPMC12774293

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.