Evidence map›Paper›PMID 32333774›Full record

ArticleEndocrinology2020

Mutational Analysis of the Putative Anti-Müllerian Hormone (AMH) Binding Interface on its Type II Receptor, AMHR2.

Kaitlin N Hart, David Pépin, Magdalena Czepnik, Patricia K Donahoe, Thomas B Thompson

Open access · hybridAbstract read
In one paragraph

Article in Endocrinology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. A divergent two-domain structure of the anti-Müllerian hormone prodomain.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Genetic insights into the complexity of premature ovarian insufficiency.Reproductive biology and endocrinology : RB&E · 2024
    Review
  3. Article
  4. Characterization of the molecular mechanisms that govern anti-Müllerian hormone synthesis and activity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  5. Review
  6. Review
  7. Molecular Mechanisms of AMH Signaling.Frontiers in endocrinology · 2022
    Review
  8. Review
  9. Structure of AMH bound to AMHR2 provides insight into a unique signaling pair in the TGF-β family.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. 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

5 authors at 2 institutions in 1 country.

Kaitlin N HartDepartment of Pharmacology and Systems Physiology, University of Cincinnati, Cincinnati, OH, USA.
David PépinDepartment of Surgery, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
Magdalena CzepnikDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, OH, USA.
Patricia K DonahoeDepartment of Surgery, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
Thomas B ThompsonDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, OH, USA.
University of Cincinnati · USHarvard University · US

Funding

ENVIRONMETAL CARCINOGENESIS AND MUTAGENESIST32ES007250 · NIEHS · UNIVERSITY OF CINCINNATI · PI MILLER, WILLIAM E · 1988 to 2024
$11.9M
NIEHS NIH HHS T32 ES007250
6 · The paper itself

Abstract

Anti-Müllerian hormone (AMH) or Müllerian inhibiting substance is a unique member of the TGF-β family responsible for development and differentiation of the reproductive system. AMH signals through its own dedicated type II receptor, anti-Müllerian hormone receptor type II (AMHR2), providing an exclusive ligand-receptor pair within the broader TGF-β family. In this study, we used previous structural information to derive a model of AMH bound to AMHR2 to guide mutagenesis studies to identify receptor residues important for AMH signaling. Nonconserved mutations were introduced in AMHR2 and characterized in an AMH-responsive cell-based luciferase assay and native PAGE. Collectively, our results identified several residues important for AMH signaling within the putative ligand binding interface of AMHR2. Our results show that AMH engages AMHR2 at a similar interface to how activin and BMP class ligands bind the type II receptor, ACVR2B; however, there are significant molecular differences at the ligand interface of these 2 receptors, where ACVR2B is mostly hydrophobic and AMHR2 is predominately charged. Overall, this study shows that although the location of ligand binding on the receptor is similar to ACVR2A, ACVR2B, and BMPR2; AMHR2 uses unique ligand-receptor interactions to impart specificity for AMH.

Indexed as

Activin Receptors, Type IIAnti-Mullerian HormoneDisorder of Sex Development, 46,XYHEK293 CellsHumansMutagenesis, Site-DirectedReceptors, PeptideReceptors, Transforming Growth Factor betaActivin Receptors, Type IIACVR2B protein, humanAnti-Mullerian Hormoneanti-Mullerian hormone receptorReceptors, PeptideReceptors, Transforming Growth Factor betaAMHR2anti-Müllerian Hormone (AMH)ligand-receptor interactionsMISR2mutagenesistransforming growth factor beta (TGF-β)

Identifiers

PMID32333774
PMCPMC7286617
OpenAlexW3018986841

What OpenQuestion holds

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Registered trials

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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.