BAIT

PKC1

CLY15, CLY5, CLY7, HPO2, STT1, protein kinase C, L000001446, L000000362, S000029091, YBL105C
Protein serine/threonine kinase; essential for cell wall remodeling during growth; localized to sites of polarized growth and the mother-daughter bud neck; homolog of the alpha, beta, and gamma isoforms of mammalian protein kinase C (PKC)
Saccharomyces cerevisiae (S288c)
PREY

FAR1

cyclin-dependent protein serine/threonine kinase inhibiting protein FAR1, L000000600, YJL157C
CDK inhibitor and nuclear anchor; during the cell cycle Far1p sequesters the GEF Cdc24p in the nucleus; phosphorylation by Cdc28p-Cln results in SCFCdc4 complex-mediated ubiquitin-dependent degradation, releasing Cdc24p for export and activation of GTPase Cdc42p; in response to pheromone, phosphorylation of Far1p by MAPK Fus3p results in association with, and inhibition of Cdc28p-Cln, as well as Msn5p mediated nuclear export of Far1p-Cdc24p, targeting Cdc24p to polarity sites
Saccharomyces cerevisiae (S288c)

Biochemical Activity (Phosphorylation)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

Mechanical stress impairs pheromone signaling via Pkc1-mediated regulation of the MAPK scaffold Ste5.

van Drogen F, Mishra R, Rudolf F, Walczak MJ, Lee SS, Reiter W, Hegemann B, Pelet S, Dohnal I, Binolfi A, Yudina Z, Selenko P, Wider G, Ammerer G, Peter M

Cells continuously adapt cellular processes by integrating external and internal signals. In yeast, multiple stress signals regulate pheromone signaling to prevent mating under unfavorable conditions. However, the underlying crosstalk mechanisms remain poorly understood. Here, we show that mechanical stress activates Pkc1, which prevents lysis of pheromone-treated cells by inhibiting polarized growth. In vitro Pkc1 phosphorylates conserved residues within the RING-H2 ... [more]

J Cell Biol Dec. 02, 2018; 218(9);3117-3133 [Pubmed: 31315942]

Throughput

  • Low Throughput

Curated By

  • BioGRID