Evidence map›Paper›PMID 30321401›Full record

ArticleNucleic acids research2018

Structural basis for receptor-regulated SMAD recognition by MAN1.

Ken-Ichi Miyazono, Yosuke Ohno, Hikaru Wada, Tomoko Ito, Yui Fukatsu, Akira Kurisaki, Makoto Asashima, Masaru Tanokura

Abstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. The Role of Bone Morphogenetic Protein 4 in Ovarian Function and Diseases.Reproductive sciences (Thousand Oaks, Calif.) · 2021
    Review
  8. DiffBond: A Method for Predicting Intermolecular Bond Formation.Proceedings. IEEE International Conference on Bioinformatics and Biomedicine · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Structural biology of the TGFβ family.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
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.

Ken-Ichi MiyazonoDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.
Yosuke OhnoDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.
Hikaru WadaDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.
Tomoko ItoDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.
Yui FukatsuGraduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
Akira KurisakiGraduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
Makoto AsashimaBiotechnology Research Institute for Drug Discovery (BRD), National Institute of Advanced Industrial Science and Technology (AIST), Ibaraki, Japan.
Masaru TanokuraDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Receptor-regulated SMAD (R-SMAD: SMAD1, SMAD2, SMAD3, SMAD5 and SMAD8) proteins are key transcription factors of the transforming growth factor-β (TGF-β) superfamily of cytokines. MAN1, an integral protein of the inner nuclear membrane, is a SMAD cofactor that terminates TGF-β superfamily signals. Heterozygous loss-of-function mutations in MAN1 result in osteopoikilosis, Buschke-Ollendorff syndrome and melorheostosis. MAN1 interacts with MAD homology 2 (MH2) domains of R-SMAD proteins using its C-terminal U2AF homology motif (UHM) domain and UHM ligand motif (ULM) and facilitates R-SMAD dephosphorylation. Here, we report the structural basis for R-SMAD recognition by MAN1. The SMAD2-MAN1 and SMAD1-MAN1 complex structures show that an intramolecular UHM-ULM interaction of MAN1 forms a hydrophobic surface that interacts with a hydrophobic surface among the H2 helix, the strands β8 and β9, and the L3 loop of the MH2 domains of R-SMAD proteins. The complex structures also show the mechanism by which SMAD cofactors distinguish R-SMAD proteins that possess a highly conserved molecular surface.

Indexed as

Amino Acid MotifsAnimalsComputer SimulationCrystallography, X-RayCytokinesDNA-Binding ProteinsDNA Mutational AnalysisHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsMembrane ProteinsMutationNuclear EnvelopeNuclear ProteinsPhosphorylationProtein BindingCytokinesDNA-Binding ProteinsLEMD3 protein, humanMembrane ProteinsNuclear ProteinsSmad1 ProteinSMAD1 protein, humanSmad2 ProteinSMAD2 protein, humanSmad3 ProteinSMAD3 protein, humanTransforming Growth Factor beta

Identifiers

PMID30321401
PMCPMC6294489

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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.