Evidence map›Paper›PMID 16908671›Full record

ArticleThe Journal of cell biology2006

Plectin-controlled keratin cytoarchitecture affects MAP kinases involved in cellular stress response and migration.

Selma Osmanagic-Myers, Martin Gregor, Gernot Walko, Gerald Burgstaller, Siegfried Reipert, Gerhard Wiche

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

89 citing papers in PubMed, 165 citations in OpenAlex.

  1. Article
  2. Article
  3. SRC and ERK Regulate the Turnover of Cytoskeletal Keratin Filaments.International journal of molecular sciences · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. [Plectin Promotes the Migration of Hepatocellular Carcinoma Cells Through Inducing F-actin Polymerization].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2024
    Article
  9. Role of plectin and its interacting molecules in cancer.Medical oncology (Northwood, London, England) · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Susceptibility of cytoskeletal-associated proteins for tumor progression.Cellular and molecular life sciences : CMLS · 2021
    Review
  16. Keratins as an Inflammation Trigger Point in Epidermolysis Bullosa Simplex.International journal of molecular sciences · 2021
    Review
  17. Review
  18. Review
  19. Review
  20. Review

29 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Selma Osmanagic-MyersDepartment of Molecular Cell Biology, Max F. Perutz Laboratories, University of Vienna, A-1030 Vienna, Austria.
Martin Gregor
Gernot Walko
Gerald Burgstaller
Siegfried Reipert
Gerhard Wiche
Max Perutz Labs · ATUniversity of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plectin is a major intermediate filament (IF)-based cytolinker protein that stabilizes cells and tissues mechanically, regulates actin filament dynamics, and serves as a scaffolding platform for signaling molecules. In this study, we show that plectin deficiency is a cause of aberrant keratin cytoskeleton organization caused by a lack of orthogonal IF cross-linking. Keratin networks in plectin-deficient cells were more susceptible to osmotic shock-induced retraction from peripheral areas, and their okadaic acid-induced disruption (paralleled by stress-activated MAP kinase p38 activation) proceeded faster. Basal activities of the MAP kinase Erk1/2 and of the membrane-associated upstream protein kinases c-Src and PKCdelta were significantly elevated, and increased migration rates, as assessed by in vitro wound-closure assays and time-lapse microscopy, were observed. Forced expression of RACK1, which is the plectin-binding receptor protein for activated PKCdelta, in wild-type keratinocytes elevated their migration potential close to that of plectin-null cells. These data establish a link between cytolinker-controlled cytoarchitecture/scaffolding functions of keratin IFs and specific MAP kinase cascades mediating distinct cellular responses.

Indexed as

AnimalsCell MovementCytoskeletonEnzyme InhibitorsIntermediate Filament ProteinsKeratinocytesKeratinsMAP Kinase Signaling SystemMiceMice, KnockoutMicroscopy, Electron, TransmissionMitogen-Activated Protein Kinase 3NeuropeptidesOkadaic AcidOsmotic Pressurep38 Mitogen-Activated Protein KinasesEnzyme InhibitorsIntermediate Filament ProteinsKeratinsMitogen-Activated Protein Kinase 3NeuropeptidesOkadaic Acidp38 Mitogen-Activated Protein KinasesPlakinsPlec protein, mousePlectinProtein Kinase C-deltaRACK1 protein, mouseReceptors for Activated C Kinasesrc-Family Kinases

Identifiers

PMID16908671
PMCPMC2064261
OpenAlexW2151891310

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.