BAIT
SOG2
YOR353C
Key component of the RAM signaling network; required for proper cell morphogenesis and cell separation after mitosis
GO Process (3)
GO Function (0)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
CBK1
serine/threonine protein kinase CBK1, L000004609, YNL161W
Serine/threonine protein kinase of the the RAM signaling network; Ndr/LATS family member; binds regulatory subunit Mob2p; involved in regulation of cellular morphogenesis, polarized growth, and septum destruction; phosphorylation by Cbk1p regulates localization and activity of Ace2p transcription factor and Ssd1p translational repressor; Cbk1p activity is regulated by both phosphorylation and specific localization; relocalizes to cytoplasm upon DNA replication stress
GO Process (6)
GO Function (1)
GO Component (9)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
Phenotypic Enhancement
A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.
Publication
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 ... [more]
Mol. Genet. Genomics Feb. 01, 2010; 283(2);111-22 [Pubmed: 19967545]
Throughput
- Low Throughput
Ontology Terms
- protein/peptide accumulation (APO:0000149)
- protein/peptide distribution (APO:0000209)
Additional Notes
- double mutants show suppression of the protein aggregation phenotype seen in the single mutant
Related interactions
Curated By
- BioGRID