Mutations in the C-terminus of the conserved NDR kinase, Cbk1p of Saccharomyces cerevisiae, make the protein independent of upstream activators
Copyright policy )Mutations in the C-terminus of the conserved NDR kinase, Cbk1p of Saccharomyces cerevisiae, make the protein independent of upstream activators
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.
- University of Paris-Saclay France
- University of Paris France
- Centre national de la recherche scientifique France
- Sorbonne University France
- Sorbonne Paris Cité France
Saccharomyces cerevisiae Proteins, Intracellular Signaling Peptides and Proteins, Cell Polarity, Saccharomyces cerevisiae, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, DNA-Binding Proteins, Enzyme Activation, Repressor Proteins, Suppression, Genetic, Amino Acid Substitution, Mutation, Phosphorylation, Conserved Sequence, Metabolic Networks and Pathways, Adaptor Proteins, Signal Transducing, Transcription Factors
Saccharomyces cerevisiae Proteins, Intracellular Signaling Peptides and Proteins, Cell Polarity, Saccharomyces cerevisiae, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, DNA-Binding Proteins, Enzyme Activation, Repressor Proteins, Suppression, Genetic, Amino Acid Substitution, Mutation, Phosphorylation, Conserved Sequence, Metabolic Networks and Pathways, Adaptor Proteins, Signal Transducing, Transcription Factors
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).15 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Average influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Average impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
Citations provided by BIP!Popularity provided by BIP!