Evidence map›Paper›PMID 36045259›Full record

ArticleCellular and molecular life sciences : CMLS2022

Keratin 8 is a scaffolding and regulatory protein of ERAD complexes.

Iwona Maria Pranke, Benoit Chevalier, Aiswarya Premchandar, Nesrine Baatallah, Kamil F Tomaszewski, Sara Bitam, Danielle Tondelier, Anita Golec, Jan Stolk, Gergely L Lukacs and 9 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.6field-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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

19 authors at 6 institutions in 5 countries.

Iwona Maria PrankeInserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France. iwona.pranke@inserm.fr.
Benoit Chevalier *Inserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France.
Aiswarya Premchandar *Laboratory of Mass Spectrometry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02106, Warsaw, Poland.
Nesrine BaatallahInserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France.
Kamil F TomaszewskiInserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France.
Sara BitamInserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France.
Danielle TondelierInserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France.
Anita GolecInserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France.
Jan StolkDepartment of Pulmonology, Leiden University Medical Center, Leiden, The Netherlands.
Gergely L LukacsDepartment of Physiology, McGill University, Montréal, QC, Canada.
Pieter S HiemstraDepartment of Pulmonology, Leiden University Medical Center, Leiden, The Netherlands.
Michal DadlezLaboratory of Mass Spectrometry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02106, Warsaw, Poland.
David A LomasUCL Respiratory and the Institute of Structural and Molecular Biology, University College London, London, WC1E 6JF, UK.
James A IrvingUCL Respiratory and the Institute of Structural and Molecular Biology, University College London, London, WC1E 6JF, UK.
Agnes Delaunay-MoisanInstitute for Integrative Biology of the Cell (I2BC), Université Paris-Saclay, CEA, CNRS, Gif-sur-Yvette, France.
Eelco van AnkenDivision of Genetics and Cell Biology, San Raffaele Scientific Institute, Milan, Italy.
Alexandre Hinzpeter *Inserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France.
Isabelle Sermet-Gaudelus *Inserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France.
Aleksander EdelmanInserm, U1151, CNRS UMR 8253, Université de Paris, 160 rue de Vaugirard, 75015, Paris, France. aleksander.edelman@inserm.fr.ORCID http://orcid.org/0000-0001-6627-4264
Centre National de la Recherche Scientifique · FRInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLInstitute of Structural and Molecular Biology · GBLeiden University Medical Center · NLHôpital Necker-Enfants Malades · FRMcGill University · CA

Funding

Agence Nationale de la Recherche ANR-13-BSV1-0019-01Agence Nationale de la Recherche ANR-18-CE14-0004Chancellerie des Universités de Paris 15LEG005_9UMS1151
6 · The paper itself

Abstract

Early recognition and enhanced degradation of misfolded proteins by the endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD) cause defective protein secretion and membrane targeting, as exemplified for Z-alpha-1-antitrypsin (Z-A1AT), responsible for alpha-1-antitrypsin deficiency (A1ATD) and F508del-CFTR (cystic fibrosis transmembrane conductance regulator) responsible for cystic fibrosis (CF). Prompted by our previous observation that decreasing Keratin 8 (K8) expression increased trafficking of F508del-CFTR to the plasma membrane, we investigated whether K8 impacts trafficking of soluble misfolded Z-A1AT protein. The subsequent goal of this study was to elucidate the mechanism underlying the K8-dependent regulation of protein trafficking, focusing on the ERAD pathway. The results show that diminishing K8 concentration in HeLa cells enhances secretion of both Z-A1AT and wild-type (WT) A1AT with a 13-fold and fourfold increase, respectively. K8 down-regulation triggers ER failure and cellular apoptosis when ER stress is jointly elicited by conditional expression of the µ

Indexed as

Cystic Fibrosis Transmembrane Conductance RegulatorEndoplasmic Reticulum-Associated DegradationHeLa CellsHumansKeratin-8Transcription FactorsUbiquitin-Protein LigasesCystic Fibrosis Transmembrane Conductance RegulatorKeratin-8Transcription FactorsUbiquitin-Protein LigasesCytoskeletonEpitheliumIntermediary filamentsProtein complexes fractionationProtein–protein interactionSynthetic lethality

Identifiers

PMID36045259
PMCPMC11803007
OpenAlexW4293919856

What Socratic 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 Socratic graph.