Evidence map›Paper›PMID 35736809›Full record

ArticleeLife2022

The orphan ligand, activin C, signals through activin receptor-like kinase 7.

Erich J Goebel, Luisina Ongaro, Emily C Kappes, Kylie Vestal, Elitza Belcheva, Roselyne Castonguay, Ravindra Kumar, Daniel J Bernard, Thomas B Thompson

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.2field-weighted citation impact, top 7% of its field
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

26 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
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  6. Activin Actions in Adipocytes.The Journal of clinical endocrinology and metabolism · 2025
    Review
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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 at 3 institutions in 2 countries.

Erich J GoebelDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, United States.ORCID 0000-0001-5549-9425
Luisina OngaroDepartment of Pharmacology and Therapeutics, Centre for Research in Reproduction and Development, McGill University, Montreal, Canada.
Emily C KappesDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, United States.ORCID 0000-0002-3063-3373
Kylie VestalDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, United States.
Elitza BelchevaMerck &Co., Inc., Kenilworth, United States.
Roselyne CastonguayMerck &Co., Inc., Kenilworth, United States.
Ravindra KumarMerck &Co., Inc., Kenilworth, United States.
Daniel J BernardDepartment of Pharmacology and Therapeutics, Centre for Research in Reproduction and Development, McGill University, Montreal, Canada.ORCID 0000-0001-5365-5586
Thomas B ThompsonDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, United States.ORCID 0000-0002-7041-5047
University of Cincinnati · USMerck & Co., Inc., Rahway, NJ, USA (United States) · USMcGill University · CA

Funding

Structural/functional characterization of TGFβ superfamily signaling and regulationR35GM134923 · NIGMS · UNIVERSITY OF CINCINNATI · PI THOMPSON, THOMAS B · 2020 to 2024
$2.6M
NIGMS NIH HHS R35 GM134923
6 · The paper itself

Abstract

Activin ligands are formed from two disulfide-linked inhibin β (Inhβ) subunit chains. They exist as homodimeric proteins, as in the case of activin A (ActA; InhβA/InhβA) or activin C (ActC; InhβC/InhβC), or as heterodimers, as with activin AC (ActAC; InhβA:InhβC). While the biological functions of ActA and activin B (ActB) have been well characterized, little is known about the biological functions of ActC or ActAC. One thought is that the InhβC chain functions to interfere with ActA production by forming less active ActAC heterodimers. Here, we assessed and characterized the signaling capacity of ligands containing the InhβC chain. ActC and ActAC activated SMAD2/3-dependent signaling via the type I receptor, activin receptor-like kinase 7 (ALK7). Relative to ActA and ActB, ActC exhibited lower affinity for the cognate activin type II receptors and was resistant to neutralization by the extracellular antagonist, follistatin. In mature murine adipocytes, which exhibit high ALK7 expression, ActC elicited a SMAD2/3 response similar to ActB, which can also signal via ALK7. Collectively, these results establish that ActC and ActAC are active ligands that exhibit a distinct signaling receptor and antagonist profile compared to other activins.

Indexed as

Activin Receptors, Type IActivinsActivin ReceptorsAnimalsLigandsMiceSignal TransductionActivin ReceptorsActivin Receptors, Type IActivinsAcvr1c protein, mouseLigandsActivinActivin Cactivin-like kinase 7Adipocytebiochemistrychemical biologyhumanmouseSignalingtransforming growth factor beta

Identifiers

PMID35736809
PMCPMC9224996
OpenAlexW4283322170

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.