Evidence map›Paper›PMID 27703004›Full record

ArticleThe Journal of biological chemistry2016

Quantitative Proteomics of the SMAD (Suppressor of Mothers against Decapentaplegic) Transcription Factor Family Identifies Importin 5 as a Bone Morphogenic Protein Receptor SMAD-specific Importin.

Roy Baas, Ayestha Sijm, Hetty A A M van Teeffelen, Robert van Es, Harmjan R Vos, H Th Marc Timmers

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. 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
1.2field-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

11 citing papers in PubMed, 20 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Roy BaasFrom the Departments of Molecular Cancer Research and Stem Cells, Regenerative Medicine Center, Center for Molecular Medicine, University Medical Center Utrecht, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands.
Ayestha SijmFrom the Departments of Molecular Cancer Research and Stem Cells, Regenerative Medicine Center, Center for Molecular Medicine, University Medical Center Utrecht, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands.
Hetty A A M van TeeffelenFrom the Departments of Molecular Cancer Research and Stem Cells, Regenerative Medicine Center, Center for Molecular Medicine, University Medical Center Utrecht, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands.
Robert van EsFrom the Departments of Molecular Cancer Research and Stem Cells, Regenerative Medicine Center, Center for Molecular Medicine, University Medical Center Utrecht, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands.
Harmjan R VosFrom the Departments of Molecular Cancer Research and Stem Cells, Regenerative Medicine Center, Center for Molecular Medicine, University Medical Center Utrecht, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands.
H Th Marc TimmersFrom the Departments of Molecular Cancer Research and Stem Cells, Regenerative Medicine Center, Center for Molecular Medicine, University Medical Center Utrecht, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands H.T.M.Timmers@umcutrecht.nl.
University Medical Center Utrecht · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gene-specific transcription factors (GSTFs) control gene transcription by DNA binding and specific protein complex recruitment, which regulates promoter accessibility for transcription initiation by RNA polymerase II. Mutations in the GSTFs Suppressor of Mothers Against Decapentaplegic 2 (SMAD2) and SMAD4 are frequently associated with colon and rectal carcinomas. These proteins play an important role in bone morphogenic protein (BMP) and transforming growth factor β (TGF-β) signaling pathways controlling cell fate and proliferation. To study the protein interactome of the SMAD protein family we generated a quantitative proteomics pipeline that allows for inducible expression of GFP-tagged SMAD proteins followed by affinity purification and quantitative mass spectrometry analysis. Data are available via ProteomeXchange with identifier PXD004529. The nuclear importin IPO5 was identified as a novel interacting protein of SMAD1. Overexpression of IPO5 in various cell lines specifically increases nuclear localization of BMP receptor-activated SMADs (R-SMADs) confirming a functional relationship between IPO5 and BMP but not TGF-β R-SMADs. Finally, we provide evidence that variation in length of the lysine stretch of the nuclear localization sequence is a determinant for importin specificity.

Indexed as

beta KaryopherinsBone Morphogenetic Protein ReceptorsCell NucleusHeLa CellsHumansProteomicsSmad1 ProteinSmad2 ProteinSmad4 Proteinbeta KaryopherinsBone Morphogenetic Protein ReceptorsIPO5 protein, humanSmad1 ProteinSMAD1 protein, humanSmad2 ProteinSMAD2 protein, humanSmad4 ProteinSMAD4 protein, humanmass spectrometry (MS)nuclear translocationproteomicsSMAD transcription factortranscription regulation

Identifiers

PMID27703004
PMCPMC5104937
OpenAlexW2528032825

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.