Evidence map›Paper›PMID 8609167›Full record

ArticleThe Journal of cell biology1996

14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor.

J Liao, M B Omary

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
6.3field-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

68 citing papers in PubMed, 210 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021
    Review
  6. Intermediate filaments as effectors of differentiation.Current opinion in cell biology · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Liver disease-associated keratin 8 and 18 mutations modulate keratin acetylation and methylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  12. Article
  13. Article
  14. Modulation of epithelial cell polarity by bacterial pathogens.Annals of the New York Academy of Sciences · 2017
    Review
  15. Article
  16. Article
  17. Intermediate filament dynamics: What we can see now and why it matters.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  18. Review
  19. Review
  20. Article

8 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

2 authors at 1 institution in 1 country.

J LiaoVA Palo Alto Health Care System, CA 94304, USA.
M B Omary
VA Palo Alto Health Care System · US

Funding

Keratin Biology and Disease Aspects in Simple EpitheliaR01DK047918 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 1995 to 2018
$6.6M
GASTROINTESTINAL MEMBRANE RECEPTORSP30DK038707 · NIDDK · STANFORD UNIVERSITY · PI GREENBERG, HARRY B · 1987 to 1997
–
NIDDK NIH HHS DK38707NIDDK NIH HHS DK47918
6 · The paper itself

Abstract

14-3-3 is a ubiquitous protein family that interacts with several signal transduction kinases. We show that 14-3-3 proteins associate with keratin intermediate filament polypeptides 8 and 18 (K8/18) that are expressed in simple-type epithelia. The association is stoichiometrically significant (> or = one 14-3-3 molecule/keratin tetramer), occurs preferentially with K18, and is phosphorylation- and cell cycle-dependent in that it occurs during S/G2/M phases of the cell cycle when keratins become hyperphosphorylated. Binding of phospho-K8/18 to 14-3-3 can be reconstituted in vitro using recombinant 14-3-3 or using total cellular cytosol. Phosphatase treatment results in dissociation of 14-3-3, and dephosphorylation of phospho-K8/18 prevents reconstitution of the binding. Three cellular keratin subpopulations were analyzed that showed parallel gradients of keratin phosphorylation and 14-3-3 binding. Incubation of 14-3-3 with keratins during or after in vitro filament assembly results in sequestering of additional soluble keratin, only in cases when the keratins were hyperphosphorylated. Our results demonstrate a stoichiometrically significant cell cycle- and phosphorylation-regulated binding of 14-3-3 proteins to K18 and in vitro evidence of a simple epithelial keratin sequestering role for 14-3-3 proteins.

Indexed as

Tyrosine 3-Monooxygenase14-3-3 ProteinsAmino Acid SequenceAnimalsCell CycleCells, CulturedColonCytosolDogsEpitheliumHumansIntermediate FilamentsKeratinsMolecular Sequence DataPhosphorylationProtein Binding14-3-3 ProteinsKeratinsProteinsTyrosine 3-Monooxygenase

Identifiers

PMID8609167
PMCPMC2120793
OpenAlexW2107295635

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.