Evidence map›Paper›PMID 19805511›Full record

ArticleMolecular and cellular biology2009

Mechanism of Mpk1 mitogen-activated protein kinase binding to the Swi4 transcription factor and its regulation by a novel caffeine-induced phosphorylation.

Andrew W Truman, Ki-Young Kim, David E Levin

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. MaAzaR, a ZnJournal of fungi (Basel, Switzerland) · 2024
    Article
  4. Journal of fungi (Basel, Switzerland) · 2022
    Article
  5. Article
  6. Substrates of the MAPK Slt2: Shaping Yeast Cell Integrity.Journal of fungi (Basel, Switzerland) · 2022
    Review
  7. Control of Gene Expression via the Yeast CWI Pathway.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Review
  10. A walk-through MAPK structure and functionality with the 30-year-old yeast MAPK Slt2.International microbiology : the official journal of the Spanish Society for Microbiology · 2021
    Review
  11. Regulation of Pkc1 Hyper-Phosphorylation by Genotoxic Stress.Journal of fungi (Basel, Switzerland) · 2021
    Article
  12. Article
  13. Article
  14. Nutrients · 2020
    Review
  15. Article
  16. Article
  17. 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

3 authors at 2 institutions in 1 country.

Andrew W TrumanDepartment of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland 21205, USA.
Ki-Young Kim
David E Levin
Johns Hopkins University · USBoston University · US

Funding

ROLE OF PROTEIN KINASE C IN YEAST GROWTH CONTROLR01GM048533 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI LEVIN, DAVID E. · 1992 to 2025
$7.8M
NIGMS NIH HHS GM48533NIGMS NIH HHS R01 GM048533
6 · The paper itself

Abstract

The Mpk1 mitogen-activated protein kinase (MAPK) of the cell wall integrity signaling pathway uses a noncatalytic mechanism to activate the SBF (Swi4/Swi6) transcription factor. Active Mpk1 forms a complex with Swi4, the DNA-binding subunit of SBF, conferring the ability to bind DNA. Because SBF activation is independent of Mpk1 catalytic activity but requires Mpk1 to be in an active conformation, we sought to understand how Mpk1 interacts with Swi4. Mutational analysis revealed that binding and activation of Swi4 by Mpk1 requires an intact D-motif-binding site, a docking surface common to MAPKs that resides distal to the phosphorylation loop but does not require the substrate-binding site, revealing a novel mechanism for MAPK target regulation. Additionally, we found that Mpk1 binds near the autoinhibitory C terminus of Swi4, suggesting an activation mechanism in which Mpk1 substitutes for Swi6 in promoting Swi4 DNA binding. Finally, we show that caffeine is an atypical activator of cell wall integrity signaling, because it induces phosphorylation of the Mpk1 C-terminal extension at Ser423 and Ser428. These phosphorylations were dependent on the DNA damage checkpoint kinases, Mec1/Tel1 and Rad53. Phosphorylation of Ser423 specifically blocked SBF activation by preventing Mpk1 association with Swi4, revealing a novel mechanism for regulating MAPK target specificity.

Indexed as

AllelesCaffeineCell Cycle ProteinsCell WallCheckpoint Kinase 2DNA-Binding ProteinsGlucosyltransferasesIntracellular Signaling Peptides and ProteinsMembrane ProteinsMitogen-Activated Protein KinasesModels, MolecularMutationPhosphodiesterase InhibitorsPhosphorylationProtein BindingProtein Serine-Threonine KinasesCaffeineCell Cycle ProteinsCheckpoint Kinase 2DNA-Binding ProteinsGlucosyltransferasesGSC2 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeMembrane ProteinsMitogen-Activated Protein KinasesPhosphodiesterase InhibitorsProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSerineSLT2 protein, S cerevisiaeSWI4 protein, S cerevisiaeTEL1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID19805511
PMCPMC2786871
OpenAlexW2121897615

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.