Evidence map›Paper›PMID 39657262›Full record

ArticleGenetics2025

The C. elegans LON-1 protein requires its CAP domain for function in regulating body size and BMP signaling.

Maria Victoria Serrano, Stéphanie Cottier, Lianzijun Wang, Sergio Moreira-Antepara, Anthony Nzessi, Zhiyu Liu, Byron Williams, Myeongwoo Lee, Roger Schneiter, Jun Liu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Genetics, 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. Two novel paralogousmicroPublication biology · 2026
    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

10 authors.

Maria Victoria SerranoDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Stéphanie CottierDepartment of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.
Lianzijun WangDepartment of Biology, Baylor University, Waco, TX 76798, USA.
Sergio Moreira-AnteparaDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Anthony NzessiDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Zhiyu LiuDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Byron WilliamsDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Myeongwoo LeeDepartment of Biology, Baylor University, Waco, TX 76798, USA.ORCID 0000-0003-2652-3646
Roger SchneiterDepartment of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.
Jun LiuDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0001-7815-4075

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Ann E. Rougvie · 2012 to 2026
$7.5M
Molecular Mechanisms Regulating and Interpreting BMP SignalingR35GM130351 · NIGMS · CORNELL UNIVERSITY · PI Jun Liu · 2019 to 2026
$4.3M
Baylor UniversityC. elegans Genetics CenterNIGMS NIH HHS R35 GM130351NIH HHS GM130351NIH HHS P40 OD010440Research Infrastructure Programs P40 OD-010440Swiss National Science Foundation 310030_207870URSA
6 · The paper itself

Abstract

The CAP (cysteine-rich secretory proteins, antigen-5, and pathogenesis-related) proteins are widely expressed and have been implicated to play diverse roles ranging from mammalian reproduction to plant immune response. Increasing evidence supports a role of CAP proteins in lipid binding. The Caenorhabditis elegans CAP protein LON-1 is known to regulate body size and bone morphogenetic protein (BMP) signaling. LON-1 is a secreted protein with a conserved CAP domain and a C-terminal unstructured domain with no homology to other proteins. In this study, we report that the C-terminal domain of LON-1 is dispensable for its function. Instead, key conserved residues located in the CAP domain are critical for LON-1 function in vivo. We further showed that LON-1 is capable of binding sterol, but not fatty acid, in vitro, and that certain key residues implicated in LON-1 function in vivo are also important for LON-1 sterol binding in vitro. These findings suggest a role of LON-1 in regulating body size and BMP signaling via sterol binding.

Indexed as

Body SizeBone Morphogenetic ProteinsCaenorhabditis elegansCaenorhabditis elegans ProteinsSignal TransductionAnimalsProtein BindingProtein DomainsBone Morphogenetic ProteinsCaenorhabditis elegans ProteinsBMP signalingbody sizeCAPC. elegansfatty acid bindingLON-1sterol binding

Identifiers

PMID39657262
PMCPMC11796460

What Socratic 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 Socratic graph.