Evidence map›Paper›PMID 15899852›Full record

ArticleMolecular and cellular biology2005

Raf-1 serine 338 phosphorylation plays a key role in adhesion-dependent activation of extracellular signal-regulated kinase by epidermal growth factor.

Matthew L Edin, Rudy L Juliano

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.1field-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

30 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. SHOC2 complex-driven RAF dimerization selectively contributes to ERK pathway dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Article
  7. PIK3CAOncotarget · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. PAK signaling in cancer.Cellular logistics · 2012
    Article
  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.

Matthew L EdinDepartment of Pharmacology, University of North Carolina, Chapel Hill, 1017 Mary Ellen Jones Building, CB 7365, Chapel Hill, NC 27599-7365, USA.
Rudy L Juliano
University of North Carolina at Chapel Hill · US

Funding

MOLECULAR BASES OF CELL ADHESIONR01GM026165 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JULIANO, RUDOLPH · 1985 to 2003
$1.0M
NHLBI NIH HHS HL4500NIGMS NIH HHS GM26165NIGMS NIH HHS R01 GM026165
6 · The paper itself

Abstract

Activation of the extracellular signal-regulated kinase (ERK) 1/2 cascade by polypeptide growth factors is tightly coupled to adhesion to extracellular matrix in nontransformed cells. Raf-1, the initial kinase in this cascade, is intricately regulated by phosphorylation, localization, and molecular interactions. We investigated the complex interactions between Raf-1, protein kinase A (PKA), and p21-activated kinase (PAK) to determine their roles in the adhesion dependence of signaling from epidermal growth factor (EGF) to ERK. We conclude that Raf-1 phosphorylation on serine 338 (S338) is a critical step that is inhibited in suspended cells. Restoration of phosphorylation at S338, either by expression of highly active PAK or by expression of an S338 phospho-mimetic Raf-1 mutation, led to a partial rescue of ERK activation in suspended cells. Raf-1 inhibition in suspension was not due to excessive negative regulation on inhibitory sites S43 and S259, as these serines were largely dephosphorylated in suspended cells. Finally, strong phosphorylation of Raf-1 S338 provided resistance to PKA-mediated inhibition of ERK activation. Phosphorylation at Raf-1 S43 and S259 by PKA only weakly inhibited EGF activation of Raf-1 and ERK when cells maintained high Raf-1 S338 phosphorylation.

Indexed as

Cell AdhesionAnimalsCell LineCell MembraneEnzyme ActivationEpidermal Growth FactorExtracellular MatrixHumansMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3PhosphorylationProto-Oncogene Proteins c-rafRNA, Small InterferingSerineSignal TransductionEpidermal Growth FactorMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Proto-Oncogene Proteins c-rafRNA, Small InterferingSerine

Identifiers

PMID15899852
PMCPMC1140616
OpenAlexW2114901751

What OpenQuestion 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 OpenQuestion graph.