Evidence map›Paper›PMID 19967545›Full record

ArticleMolecular genetics and genomics : MGG2010

Mutations in the C-terminus of the conserved NDR kinase, Cbk1p of Saccharomyces cerevisiae, make the protein independent of upstream activators.

Cristina Panozzo, Myriam Bourens, Aleksandra Nowacka, Christopher James Herbert

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Article in Molecular genetics and genomics : MGG, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

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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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. MST kinases in development and disease.The Journal of cell biology · 2015
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
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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

4 authors.

Cristina PanozzoCentre de Génétique Moléculaire du CNRS, FRE3144, FRC3115, Ave de la Terrasse, 91198, Gif-sur-Yvette, France.
Myriam Bourens
Aleksandra Nowacka
Christopher James Herbert

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Saccharomyces cerevisiae, the RAM network is involved in cell separation after cytokinesis, cell integrity and cell polarity. The key function of this network is the regulation of the activity of the protein kinase Cbk1p, which is a member of the conserved NDR kinase family. Cbk1p function is controlled by its sub-cellular localization and at least two phosphorylation events: an auto phosphorylation in the kinase domain (S570) and the phosphorylation of a C-terminal hydrophobic motif by an upstream kinase (T743). After a UV mutagenesis, we have isolated 115 independent extragenic suppressors of four ram mutations: tao3, hym1, kic1 and sog2. Over 50% of the suppressors affect a single residue in Cbk1p (S745F), which is close to the phosphorylation site in the hydrophobic motif. Our results show that the CBK1-S745F allele leads to a constitutively active form of Cbk1p that is independent of the upstream RAM network. We hypothesize that the mutant Cbk1-S745Fp mimics the effect of the phosphorylation of T743.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SubstitutionCell PolarityConserved SequenceDNA-Binding ProteinsEnzyme ActivationIntracellular Signaling Peptides and ProteinsMetabolic Networks and PathwaysMutationPhosphorylationProtein Serine-Threonine KinasesProtein Structure, TertiaryRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSuppression, GeneticACE2 protein, S cerevisiaeAdaptor Proteins, Signal TransducingCBK1 protein, S cerevisiaeDNA-Binding ProteinsHym1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesRepressor ProteinsSaccharomyces cerevisiae ProteinsTAO3 protein, S cerevisiaeTranscription Factors

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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.