PKC1/YBL105C Summary Help

Standard Name PKC1 1
Systematic Name YBL105C
Alias CLY15 2 , HPO2 3 , STT1 4 , CLY5 5 , CLY7 5
Feature Type ORF, Verified
Description 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) (6, 7, 8 and see Summary Paragraph)
Name Description Protein Kinase C 1
Chromosomal Location
ChrII:17696 to 14241 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -79 cM
Gene Ontology Annotations All PKC1 GO evidence and references
  View Computational GO annotations for PKC1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
Large-scale survey
reduction of function
424 total interaction(s) for 317 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 17
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 9
  • Biochemical Activity: 8
  • Reconstituted Complex: 3
  • Two-hybrid: 51

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Lethality: 5
  • Dosage Rescue: 74
  • Negative Genetic: 137
  • Phenotypic Enhancement: 6
  • Phenotypic Suppression: 24
  • Positive Genetic: 26
  • Synthetic Growth Defect: 7
  • Synthetic Lethality: 41
  • Synthetic Rescue: 13

Expression Summary
Length (a.a.) 1,151
Molecular Weight (Da) 131,476
Isoelectric Point (pI) 7.11
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrII:17696 to 14241 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -79 cM
Last Update Coordinates: 1996-07-31 | Sequence: 2011-02-03
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..3456 17696..14241 1996-07-31 2011-02-03
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000201

The Pkc1p kinase controls a highly-conserved cell wall integrity signalling pathway that regulates functions essential for growth and the integrity of proliferating cells (9, 10, 11). This pathway consists of a cascade of phosphorylation reactions initiated with the activation of Pkc1p (1, 2). Pkc1p then activates a basic three-protein kinase module involving an integration of the MEK-kinase Bck1p (12, 13), the redundant MEK-kinases Mkk1p and Mkk2p (14), and the MAP kinase Slt2p (15, 9). Strains disrupted for any of these protein kinases lose osmotic stability, especially at 37 C, such that the cells are viable only in the presence of sorbitol (or some other osmotic stabilizer), suggesting that the lysis is due to lack of cell wall integrity (11, 16).

Protein kinase C (PKC) is conserved throughout eukaryotes, and is highly regulated for both catalytic activity and intracellular localization (17). PKCs contain conserved regulatory motifs known as C1, C2, and HR1 domains, all of which are present in Pkc1p, the single isozyme present in S. cerevisiae (17). Pkc1p localizes to sites of polarized growth, consistent with its function in maintaining cell wall integrity, with the HR1 domain targeting it to the bud tip and the C1 domain targeting Pkc1p to the cell periphery (17). Deletion of the HR1 domain results in Pkc1p localization to the mitotic spindle with the C2 domain being responsible for this targeting (17). Pck1p activity is required for its localization to the bud neck, which also depends on the integrity of the septin ring (17). Pkc1p can also accumulate in the nucleus, and contains nuclear localization signals, as well as a nuclear exit signal (17). Therefore, it has been proposed that Pkc1p shuttles in and out of the nucleus and consequently has access to nuclear substrates (17). The nuclear and spindle localization of Pkc1p may provide a molecular explanation for previous observations suggesting a role for Pkc1p in regulating microtubule function (17).

Cercosporamide, a broad-spectrum natural antifungal compound, is a selective and highly potent fungal Pkc1p kinase inhibitor. Cells with reduced Pkc1p activity become hypersensitive to cercosporamide, and this sensitivity can be suppressed under high-osmotic growth conditions (10).

Last updated: 2005-03-22 Contact SGD

References cited on this page View Complete Literature Guide for PKC1
1) Levin DE, et al.  (1990) A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle. Cell 62(2):213-24
2) Paravicini G, et al.  (1992) The osmotic integrity of the yeast cell requires a functional PKC1 gene product. Mol Cell Biol 12(11):4896-905
3) Shimizu J, et al.  (1994) The hypo-osmolarity-sensitive phenotype of the Saccharomyces cerevisiae hpo2 mutant is due to a mutation in PKC1, which regulates expression of beta-glucanase. Mol Gen Genet 242(6):641-8
4) Yoshida S, et al.  (1992) Characterization of a staurosporine- and temperature-sensitive mutant, stt1, of Saccharomyces cerevisiae: STT1 is allelic to PKC1. Mol Gen Genet 231(3):337-44
5) Baymiller J and McCullough JE  (1997) Saccharomyces cerevisiae cell lysis mutations cly5 and cly7 define temperature-sensitive alleles of PKC1, the gene encoding yeast protein kinase C. Yeast 13(4):305-12
6) Levin DE, et al.  (1994) Dissecting the protein kinase C/MAP kinase signalling pathway of Saccharomyces cerevisiae. Cell Mol Biol Res 40(3):229-39
7) Andrews PD and Stark MJ  (2000) Dynamic, Rho1p-dependent localization of Pkc1p to sites of polarized growth. J Cell Sci 113 ( Pt 15):2685-93
8) Watanabe M, et al.  (1994) Saccharomyces cerevisiae PKC1 encodes a protein kinase C (PKC) homolog with a substrate specificity similar to that of mammalian PKC. J Biol Chem 269(24):16829-36
9) Lee KS, et al.  (1993) A yeast mitogen-activated protein kinase homolog (Mpk1p) mediates signalling by protein kinase C. Mol Cell Biol 13(5):3067-75
10) Sussman A, et al.  (2004) Discovery of cercosporamide, a known antifungal natural product, as a selective Pkc1 kinase inhibitor through high-throughput screening. Eukaryot Cell 3(4):932-43
11) Martin H, et al.  (1996) Molecular and functional characterization of a mutant allele of the mitogen-activated protein-kinase gene SLT2(MPK1) rescued from yeast autolytic mutants. Curr Genet 29(6):516-22
12) Costigan C, et al.  (1994) NHP6A and NHP6B, which encode HMG1-like proteins, are candidates for downstream components of the yeast SLT2 mitogen-activated protein kinase pathway. Mol Cell Biol 14(4):2391-403
13) Lee KS and Levin DE  (1992) Dominant mutations in a gene encoding a putative protein kinase (BCK1) bypass the requirement for a Saccharomyces cerevisiae protein kinase C homolog. Mol Cell Biol 12(1):172-82
14) Irie K, et al.  (1993) MKK1 and MKK2, which encode Saccharomyces cerevisiae mitogen-activated protein kinase-kinase homologs, function in the pathway mediated by protein kinase C. Mol Cell Biol 13(5):3076-83
15) Torres L, et al.  (1991) A protein kinase gene complements the lytic phenotype of Saccharomyces cerevisiae lyt2 mutants. Mol Microbiol 5(11):2845-54
16) Cid VJ, et al.  (1995) Molecular basis of cell integrity and morphogenesis in Saccharomyces cerevisiae. Microbiol Rev 59(3):345-86
17) Denis V and Cyert MS  (2005) Molecular analysis reveals localization of Saccharomyces cerevisiae protein kinase C to sites of polarized growth and Pkc1p targeting to the nucleus and mitotic spindle. Eukaryot Cell 4(1):36-45