Evidence map›Paper›PMID 15314064›Full record

ArticleThe Journal of cell biology2004

Raf-1 activation disrupts its binding to keratins during cell stress.

Nam-On Ku, Haian Fu, M Bishr Omary

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Calreticulin in renal fibrosis: A short review.Journal of cellular and molecular medicine · 2022
    Review
  5. Keratin 8/18 Regulate the Akt Signaling Pathway.International journal of molecular sciences · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Selective Raf inhibition in cancer therapy.Expert opinion on therapeutic targets · 2007
    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

3 authors at 2 institutions in 1 country.

Nam-On KuDepartment of Medicine, VA Palo Alto Medical Center, 3801 Miranda Ave., 154J, Palo Alto, CA 94304, USA.
Haian Fu
M Bishr Omary
Stanford University · USEmory University · US

Funding

Proteomics/GenomicsP30DK056339 · NIDDK · STANFORD UNIVERSITY · PI GREENBERG, HARRY BERNARD · 2001 to 2010
$10.4M
Regulation and Dynamics of Keratins in Digestive OrgansR01DK052951 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 1997 to 2015
$4.5M
Structure and Function of 14 3 3 ProteinsR01GM053165 · NIGMS · EMORY UNIVERSITY · PI FU, HAIAN · 2002 to 2005
$1.1M
Genetic and molecular effects on hepatocyte nucleocytoplasm protein aggregationR56DK052951 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 2012 to 2012
$179k
STRUCTURE AND FUNCTION OF 14 3 3 PROTEINSR29GM053165 · NIGMS · EMORY UNIVERSITY · PI FU, HAIAN · 1996 to 2000
$104k
NIDDK NIH HHS DK52951NIDDK NIH HHS DK56339NIDDK NIH HHS P30 DK056339NIDDK NIH HHS R01 DK052951NIDDK NIH HHS R56 DK052951NIGMS NIH HHS GM53165NIGMS NIH HHS R01 GM053165NIGMS NIH HHS R29 GM053165
6 · The paper itself

Abstract

Keratins 8 and 18 (K8/18) heteropolymers may regulate cell signaling via the known K18 association with 14-3-3 proteins and 14-3-3 association with Raf-1 kinase. We characterized Raf-keratin-14-3-3 associations and show that Raf associates directly with K8, independent of Raf kinase activity or Ras-Raf interaction, and that K18 is a Raf physiologic substrate. Raf activation during oxidative and toxin exposure in cultured cells and animals disrupt keratin-Raf association in a phosphorylation-dependent manner. Mutational analysis showed that 14-3-3 residues that are essential for Raf binding also regulate 14-3-3-keratin association. Similarly, Raf phosphorylation sites that are important for binding to 14-3-3 are also essential for Raf binding to K8/18. Therefore, keratins may modulate some aspects of Raf signaling under basal conditions via sequestration by K8, akin to Raf-14-3-3 binding. Keratin-bound Raf kinase is released upon Raf hyperphosphorylation and activation during oxidative and other stresses.

Indexed as

14-3-3 ProteinsAnimalsBinding SitesCell LineCell Line, TumorCricetinaeDNA, ComplementaryDNA Mutational AnalysisElectrophoresis, Polyacrylamide GelHumansKeratinsMiceMice, TransgenicMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein Kinases14-3-3 ProteinsDNA, ComplementaryKeratinsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesOxygenPolymersProto-Oncogene Proteins c-rafTyrosine 3-Monooxygenase

Identifiers

PMID15314064
PMCPMC2172217
OpenAlexW2037892784

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.