Evidence map›Paper›PMID 1740472›Full record

ArticleThe Journal of cell biology1992

The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells.

T S Stappenbeck, K J Green

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

52 citing papers in PubMed, 195 citations in OpenAlex.

  1. Article
  2. Article
  3. Intermediate Filaments and the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2017
    Review
  4. Physiological Functions of the Cellular Prion Protein.Frontiers in molecular biosciences · 2017
    Review
  5. Article
  6. Cell adhesion in epidermal development and barrier formation.Current topics in developmental biology · 2015
    Review
  7. Mechanistic basis of desmosome-targeted diseases.Journal of molecular biology · 2013
    Review
  8. Article
  9. Article
  10. The calcium ATPase SERCA2 regulates desmoplakin dynamics and intercellular adhesive strength through modulation of PKCα signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  11. Article
  12. Article
  13. Desmosomes in vivo.Dermatology research and practice · 2010
    Article
  14. Article
  15. Article
  16. Periplakin interactions with lens intermediate and beaded filaments.Investigative ophthalmology & visual science · 2009
    Article
  17. The desmosome and pemphigus.Histochemistry and cell biology · 2008
    Review
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

T S StappenbeckDepartment of Pathology, Northwestern University Medical School, Chicago, Illinois 60611.
K J Green
Northwestern University · US

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
HUMAN DESMOPLAKIN GENE STRUCTURE &EXPRESSION IN EMBRYOSR01HD024430 · NICHD · NORTHWESTERN UNIVERSITY · PI GREEN, KATHLEEN JANEE · 1988 to 1990
–
NICHD NIH HHS HD24430NIGMS NIH HHS T32-GM08061
6 · The paper itself

Abstract

Specific interactions between desmoplakins I and II (DP I and II) and other desmosomal or cytoskeletal molecules have been difficult to determine in part because of the complexity and insolubility of the desmosome and its constituents. We have used a molecular genetic approach to investigate the role that DP I and II may play in the association of the desmosomal plaque with cytoplasmic intermediate filaments (IF). A series of mammalian expression vectors encoding specific predicted domains of DP I were transiently expressed in cultured cells that form (COS-7) and do not form (NIH-3T3) desmosomes. Sequence encoding a small antigenic peptide was added to the 3' end of each mutant DP cDNA to facilitate immunolocalization of mutant DP protein. Light and electron microscopical observations revealed that DP polypeptides including the 90-kD carboxy-terminal globular domain of DP I specifically colocalized with and ultimately resulted in the complete disruption of IF in both cell lines. This effect was specific for IF as microtubule and microfilament networks were unaltered. This effect was also specific for the carboxyl terminus of DP, as the expression of the 95-kD rod domain of DP I did not visibly alter IF networks. Immunogold localization of COS-7 cells transfected with constructs including the carboxyl terminus of DP demonstrated an accumulation of mutant protein in perinuclear aggregates within which IF subunits were sequestered. These results suggest a role for the DP carboxyl terminus in the attachment of IF to the desmosome in either a direct or indirect manner.

Indexed as

3T3 CellsAnimalsBase SequenceCell LineChlorocebus aethiopsCytoskeletal ProteinsCytoskeletonDesmoplakinsDesmosomesGene ExpressionGenetic VectorsIntermediate Filament ProteinsMiceMolecular Sequence DataTubulinVimentinCytoskeletal ProteinsDesmoplakinsDsp protein, mouseIntermediate Filament ProteinsTubulinVimentin

Identifiers

PMID1740472
PMCPMC2289350
OpenAlexW2155244669

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.