Evidence map›Paper›PMID 22961979›Full record

ArticleThe Journal of biological chemistry2012

SMAD versus non-SMAD signaling is determined by lateral mobility of bone morphogenetic protein (BMP) receptors.

Asja Guzman, Monika Zelman-Femiak, Jan H Boergermann, Sandra Paschkowsky, Peter A Kreuzaler, Peter Fratzl, Gregory S Harms, Petra Knaus

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  11. Identification of Polysaccharides FromFrontiers in pharmacology · 2022
    Article
  12. Review
  13. Article
  14. Article
  15. The BMP Pathway in Blood Vessel and Lymphatic Vessel Biology.International journal of molecular sciences · 2021
    Review
  16. Review
  17. The Role of Bone Morphogenetic Proteins in Diabetic Complications.ACS pharmacology & translational science · 2020
    Review
  18. Article
  19. Article
  20. Palmitoylation of BMPR1a regulates neural stem cell fate.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

8 authors at 4 institutions in 3 countries.

Asja GuzmanInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Thielallee 63, 14195 Berlin, Germany.
Monika Zelman-Femiak
Jan H Boergermann
Sandra Paschkowsky
Peter A Kreuzaler
Peter Fratzl
Gregory S Harms
Petra Knaus
Freie Universität Berlin · DEUniversity of Würzburg · DEMax Planck Society · DEUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bone (or body) morphogenetic proteins (BMPs) belong to the TGFβ superfamily and are crucial for embryonic patterning and organogenesis as well as for adult tissue homeostasis and repair. Activation of BMP receptors by their ligands leads to induction of several signaling cascades. Using fluorescence recovery after photobleaching, FRET, and single particle tracking microscopy, we demonstrate that BMP receptor type I and II (BMPRI and BMPRII) have distinct lateral mobility properties within the plasma membrane, which is mandatory for their involvement in different signaling pathways. Before ligand binding, BMPRI and a subpopulation of BMPRII exhibit confined motion, reflecting preassembled heteromeric receptor complexes. A second free diffusing BMPRII population only becomes restricted after ligand addition. This paper visualizes time-resolved BMP receptor complex formation and demonstrates that the lateral mobility of BMPRI has a major impact in stabilizing heteromeric BMPRI-BMPRII receptor complexes to differentially stimulate SMAD versus non-SMAD signaling.

Indexed as

Bone Morphogenetic Protein Receptors, Type IBone Morphogenetic Protein Receptors, Type IICell MembraneHEK293 CellsHumansMultiprotein ComplexesProtein TransportSignal TransductionSmad ProteinsBMPR2 protein, humanBone Morphogenetic Protein Receptors, Type IBone Morphogenetic Protein Receptors, Type IIMultiprotein ComplexesSmad Proteins

Identifiers

PMID22961979
PMCPMC3501045
OpenAlexW2008987365

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.