Evidence map›Paper›PMID 12097147›Full record

ArticleBMC cell biology2002

A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs).

Yin Lin, Jennifer Martin, Cornelia Gruendler, Jennifer Farley, Xianwang Meng, Bi-Yu Li, Robert Lechleider, Carla Huff, Richard H Kim, William A Grasser and 2 more

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 62 citations in OpenAlex.

  1. Current updates on protein as biomarkers for diabetic kidney disease: a systematic review.Therapeutic advances in endocrinology and metabolism · 2021
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  15. The antiapoptotic DeltaNp73 is degraded in a c-Jun-dependent manner upon genotoxic stress through the antizyme-mediated pathway.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  16. Article
  17. Antizyme and antizyme inhibitor, a regulatory tango.Cellular and molecular life sciences : CMLS · 2009
    Review
  18. Article
  19. Article
  20. Expression profiling of transforming growth factor beta superfamily genes in developing orofacial tissue.Birth defects research. Part A, Clinical and molecular teratology · 2006
    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

12 authors at 5 institutions in 1 country.

Yin LinVirginia Mason Research Center, 1201 Ninth Ave, Seattle WA 98101, USA. yinlinn@yahoo.com
Jennifer Martin
Cornelia Gruendler
Jennifer Farley
Xianwang Meng
Bi-Yu Li
Robert Lechleider
Carla Huff
Richard H Kim
William A Grasser
Vishwas Paralkar
Tongwen Wang
Virginia Mason Medical Center · USNational Cancer Institute · USMassachusetts General Hospital · USPfizer (United States) · USUniversity of Washington · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe intracellular signaling events of the bone morphogenetic proteins (BMPs) involve the R-Smad family members Smad1, Smad5, Smad8 and the Co-Smad, Smad4. Smads are currently considered to be DNA-binding transcriptional modulators and shown to recruit the master transcriptional co-activator CBP/p300 for transcriptional activation. SNIP1 is a recently discovered novel repressor of CBP/p300. Currently, the detailed molecular mechanisms that allow R-Smads and Co-Smad to co-operatively modulate transcription events are not fully understood.

resultsHere we report a novel physical and functional link between Smad1 and the 26S proteasome that contributes to Smad1- and Smad4-mediated transcriptional regulation. Smad1 forms a complex with a proteasome beta subunit HsN3 and the ornithine decarboxylase antizyme (Az). The interaction is enhanced upon BMP type I receptor activation and occur prior to the incorporation of HsN3 into the mature 20S proteasome. Furthermore, BMPs trigger the translocation of Smad1, HsN3 and Az into the nucleus, where the novel CBP/p300 repressor protein SNIP1 is further recruited to Smad1/HsN3/Az complex and degraded in a Smad1-, Smad4- and Az-dependent fashion. The degradation of the CBP/p300 repressor SNIP1 is likely an essential step for Smad1-, Smad4-mediated transcriptional activation, since increased SNIP1 expression inhibits BMP-induced gene responses.

conclusionsOur studies thus add two additional important functional partners of Smad1 into the signaling web of BMPs and also suggest a novel mechanism for Smad1 and Smad4 to co-modulate transcription via regulating proteasomal degradation of CBP/p300 repressor SNIP1.

Indexed as

Intracellular Signaling Peptides and ProteinsSignal TransductionTransforming Growth Factor betaAnimalsBlotting, WesternBone Morphogenetic Protein 2Bone Morphogenetic Protein Receptors, Type IBone Morphogenetic ProteinsCarrier ProteinsCell LineCOS CellsCysteine EndopeptidasesDNA-Binding ProteinsGene Expression RegulationHumansMultienzyme ComplexesBMP2 protein, humanBone Morphogenetic Protein 2Bone Morphogenetic Protein Receptors, Type IBone Morphogenetic ProteinsCarrier ProteinsCysteine EndopeptidasesDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsMultienzyme ComplexesProteasome Endopeptidase ComplexProtein PrecursorsProtein Serine-Threonine KinasesPSMB4 protein, humanReceptors, Growth FactorRNA-Binding ProteinsSmad1 ProteinSMAD1 protein, humanSmad ProteinsSNIP1 protein, humanTrans-ActivatorsTransforming Growth Factor beta

Identifiers

PMID12097147
PMCPMC117437
OpenAlexW1502370790

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.