Evidence map›Paper›PMID 25268583›Full record

ArticleThe Journal of investigative dermatology2015

Modulation of type II TGF-β receptor degradation by integrin-linked kinase.

Linda Vi, Stellar Boo, Samar Sayedyahossein, Randeep K Singh, Sarah McLean, Gianni M Di Guglielmo, Lina Dagnino

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In one paragraph

Article in The Journal of investigative dermatology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. 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

7 authors at 3 institutions in 1 country.

Linda ViDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario, Canada; Children's Health Research Institute, Lawson Health Research Institute, University of Western Ontario, London, Ontario, Canada.
Stellar BooDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario, Canada; Children's Health Research Institute, Lawson Health Research Institute, University of Western Ontario, London, Ontario, Canada; These authors contributed equally to this work.
Samar SayedyahosseinDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario, Canada; Children's Health Research Institute, Lawson Health Research Institute, University of Western Ontario, London, Ontario, Canada.
Randeep K SinghDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario, Canada; Children's Health Research Institute, Lawson Health Research Institute, University of Western Ontario, London, Ontario, Canada.
Sarah McLeanDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario, Canada.
Gianni M Di GuglielmoDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario, Canada.
Lina DagninoDepartment of Physiology and Pharmacology, University of Western Ontario, London, Ontario, Canada; Children's Health Research Institute, Lawson Health Research Institute, University of Western Ontario, London, Ontario, Canada. Electronic address: ldagnino@uwo.ca.
Lawson Health Research Institute · CAWestern University · CAChildren’s Health Research Institute · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cutaneous responses to injury, infection, and tumor formation involve the activation of resident dermal fibroblasts and subsequent transition to myofibroblasts. The key for induction of myofibroblast differentiation is the activation of transforming growth factor-β (TGF-β) receptors and stimulation of integrins and their associated proteins, including integrin-linked kinase (ILK). Cross-talk processes between TGF-β and ILK are crucial for myofibroblast formation, as ILK-deficient dermal fibroblasts exhibit impaired responses to TGF-β receptor stimulation. We now show that ILK associates with type II TGF-β receptors (TβRII) in ligand- and receptor kinase activity-independent manners. In cells with targeted Ilk gene inactivation, cellular levels of TβRII are decreased, through mechanisms that involve enhanced ubiquitination and proteasomal degradation. Partitioning of TGF-β receptors into membrane has been linked to proteasome-dependent receptor degradation. We found that interfering with membrane raft formation in ILK-deficient cells restored TβRII levels and signaling. These observations support a model whereby ILK functions in fibroblasts to direct TβRII away from degradative pathways during their differentiation into myofibroblasts.

Indexed as

AnimalsCell DifferentiationCells, CulturedFibroblastsMiceMice, Mutant StrainsModels, AnimalMyofibroblastsProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type IIScaffold Protein ILKSignal TransductionSkinProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type IIScaffold Protein ILK

Identifiers

PMID25268583
OpenAlexW2073589535

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.