ArticleMolecular & general genetics : MGG1996
Protein-protein interactions in the yeast PKC1 pathway: Pkc1p interacts with a component of the MAP kinase cascade.
Article in Molecular & general genetics : MGG, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Differential Requirement for the Cell Wall Integrity Sensor Wsc1p in Diploids Versus Haploids.Journal of fungi (Basel, Switzerland) · 2021Article
- The Farnesyltransferase β-Subunit Ram1 RegulatesFrontiers in microbiology · 2019Article
- A framework for mapping, visualisation and automatic model creation of signal-transduction networks.Molecular systems biology · 2012Article
- Regulation of cell wall biogenesis in Saccharomyces cerevisiae: the cell wall integrity signaling pathway.Genetics · 2011Review
- Cell wall integrity signaling in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2005Review
- Automated modelling of signal transduction networks.BMC bioinformatics · 2002Article
- Osmotic stress signaling and osmoadaptation in yeasts.Microbiology and molecular biology reviews : MMBR · 2002Review
- MAP kinase pathways in the yeast Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 1998Review
- Characterization and properties of protein kinase C from the filamentous fungus Trichoderma reesei.The Biochemical journal · 1998Article
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Authors and funding
2 authors.
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Abstract
The two-hybrid system for the identification of protein-protein interactions was used to screen for proteins that interact in vivo with the Saccharomyces cerevisiae Pkc1 protein, a homolog of mammalian protein kinase C. Four positive clones were isolated that encoded portions of the protein kinase Mkk1, which acts downstream of Pkc1p in the PKC1-mediated signalling pathway. Subsequently, Pkc1p and the other PKC1 pathway components encoding members of a MAP kinase cascade, Bck1p (a MEKK), Mkk1p, Mkk2p (two functionally homologous MEKs), and Mpk1p (a MAP kinase), were tested pairwise for interaction in the two-hybrid assay. Pkc1p interacted specifically with small N-terminal deletions of Mkk1p, and no interaction between Pkc1p and any of the other known pathway components could be detected. Interaction between Pkc1p and Mkk1p, however, was found to be independent of Mkk1p kinase activity. Bck1p was also found to interact with Mkk1p and Mkk2p, and the interaction required only the predicted C-terminal catalytic domain of Mkk1p. Furthermore, we detected protein-protein interactions between two Bck1p molecules via their N-terminal regions. Finally, Mkk2p and Mpk1p also interacted in the two-hybrid assay. These results suggest that the members of the PKC1-mediated MAP kinase cascade form a complex in vivo and that Pkc1p is capable of directly interacting with at least one component of this pathway.
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