Evidence map›Paper›PMID 24337809›Full record

ArticleCellular and molecular life sciences : CMLS2014

N-linked glycosylation of the bone morphogenetic protein receptor type 2 (BMPR2) enhances ligand binding.

Jonathan W Lowery, Jose M Amich, Alex Andonian, Vicki Rosen

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.4field-weighted citation impact, top 34% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. A Novel Missense Variant ofHuman mutation · 2025
    Article
  5. Article
  6. Article
  7. Role of Glycosylation in Vascular Calcification.International journal of molecular sciences · 2021
    Review
  8. Article
  9. The Role of BMP Signaling in Endothelial Heterogeneity.Frontiers in cell and developmental biology · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. 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

4 authors at 1 institution in 1 country.

Jonathan W LoweryDepartment of Developmental Biology, Harvard School of Dental Medicine, Boston, MA, USA, jonathan_lowery@hsdm.harvard.edu.
Jose M Amich
Alex Andonian
Vicki Rosen
Harvard University · US

Funding

TRAINING GRANT IN MECHANISMS OF VASCULAR DISEASET32HL007751 · NHLBI · VANDERBILT UNIVERSITY · PI BOCK, PAUL E · 1994 to 2014
$6.6M
Adult Bone Mass Regulation by Type 2 BMP ReceptorsR01AR064227 · NIAMS · HARVARD MEDICAL SCHOOL · PI ROSEN, VICKI · 2014 to 2018
$2.6M
BMP-2 Regulation of Bone HomeostasisR01AR055904 · NIAMS · HARVARD MEDICAL SCHOOL · PI ROSEN, VICKI · 2009 to 2013
$1.9M
NHLBI NIH HHS T32 HL007751NIAMS NIH HHS R01 AR055904NIAMS NIH HHS R01AR055904NIAMS NIH HHS R01 AR064227
6 · The paper itself

Abstract

The bone morphogenetic protein (BMP) signaling pathway is essential for normal development and tissue homeostasis. BMP signal transduction occurs when ligands interact with a complex of type 1 and type 2 receptors to activate downstream transcription factors. It is well established that a single BMP receptor may bind multiple BMP ligands with varying affinity, and this has been largely attributed to conformation at the amino acid level. However, all three type 2 BMP receptors (BMPR2, ACVR2A/B) contain consensus N-glycosylation sites in their extracellular domains (ECDs), which could play a role in modulating interaction with ligand. Here, we show a differential pattern of N-glycosylation between BMPR2 and ACVR2A/B. Site-directed mutagenesis reveals that BMPR2 is uniquely glycosylated near its ligand binding domain and at a position that is mutated in patients with heritable pulmonary arterial hypertension. We further demonstrate using a cell-free pulldown assay that N-glycosylation of the BMPR2-ECD enhances its ability to bind BMP2 ligand but has no impact on binding by the closely-related ACVR2B. Our results illuminate a novel aspect of BMP signaling pathway mechanics and demonstrate a functional difference resulting from post-translational modification of type 2 BMP receptors. Additionally, since BMPR2 is required for several aspects of normal development and defects in its function are strongly implicated in human disease, our findings are likely to be relevant in several biological contexts in normal and abnormal human physiology.

Indexed as

Activin Receptors, Type IIAmino Acid SequenceBinding SitesBone Morphogenetic Protein Receptors, Type IICell LineFamilial Primary Pulmonary HypertensionGlycosylationHumansHypertension, PulmonaryLigandsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingProtein Structure, TertiaryActivin Receptors, Type IIactivin receptor type II-Aactivin receptor type II-BBMPR2 protein, humanBone Morphogenetic Protein Receptors, Type IILigands

Identifiers

PMID24337809
PMCPMC4058410
OpenAlexW2127580647

What OpenQuestion holds

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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.