PLC1/YPL268W Summary Help

Standard Name PLC1 1
Systematic Name YPL268W
Feature Type ORF, Verified
Description Phospholipase C; hydrolyzes phosphatidylinositol 4,5-biphosphate (PIP2) to generate the signaling molecules inositol 1,4,5-triphosphate (IP3) and 1,2-diacylglycerol (DAG); involved in regulating many cellular processes; Plc1p and inositol polyphosphates are required for acetyl-CoA homeostasis which regulates global histone acetylation (2, 3, 4 and see Summary Paragraph)
Name Description PhosphoLipase C 1
Chromosomal Location
ChrXVI:35236 to 37845 | ORF Map | GBrowse
Genetic position: -167.2 cM
Gene Ontology Annotations All PLC1 GO evidence and references
  View Computational GO annotations for PLC1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Classical genetics
Large-scale survey
108 total interaction(s) for 85 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 4
  • Co-purification: 1
  • Two-hybrid: 7

Genetic Interactions
  • Dosage Rescue: 7
  • Negative Genetic: 33
  • Phenotypic Enhancement: 10
  • Phenotypic Suppression: 9
  • Positive Genetic: 11
  • Synthetic Growth Defect: 13
  • Synthetic Lethality: 8
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 869
Molecular Weight (Da) 100,547
Isoelectric Point (pI) 9.84
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXVI:35236 to 37845 | ORF Map | GBrowse
Genetic position: -167.2 cM
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2610 35236..37845 1996-07-31 1996-07-31
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 SGDIDS000006189

PLC1 encodes a calcium-dependent phospholipase C that hydrolyzes phosphatidylinositol 4,5-biphosphate (PIP2) to generate the signaling molecules diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3; 1, 5). IP3 is released from the plasma membrane and is the precursor of all other inositol phosphates (IPs), an important class of signaling molecules that regulate many cellular processes (5, reviewed in 6). Plc1p activity is involved in nutrient sensing, filamentous growth, nuclear export of mRNA, actin organization, protein synthesis, kinetochore function, transcriptional regulation, vacuolar fusion, and PKA-mediated stress response (7, 8, 9, 10, 11, reviewed in 12 and 6). Little is known about the regulation of PLC1, but consensus binding sites for the transcription factors Hsf1p and Rap1p have been identified upstream of the PLC1 gene (5).

plc1 null strains have a growth defect, the severity of which is dependent on both the genetic background and the nutrient content of the media. In some strain backgrounds, the null mutant is inviable, while in other strains cell growth rate is merely reduced and inviability is seen only at higher temperatures (1, 5). Other plc1 null phenotypes include extreme sensitivity to hyperosmotic stress; increased resistance to calcium inhibition; defects in sporulation; failure to form pseudohyphae under filamentous growth-inducing conditions; increased aberrant chromosome segregation; and, when shifted to higher temperatures arrests as large, multibudded cells (5, 7 and reviewed in 12).

Phospholipase C is highly conserved from yeast to humans; homologs include S. pombe plc1 and D. discoideum pipA (reviewed in 12). Several isoforms of phospholipase C exist in mammals, and S. cerevisiae Plc1p is most similar in structure to mammalian PLC-delta (1, 5, and reviewed in 12).

Last updated: 2008-04-30 Contact SGD

References cited on this page View Complete Literature Guide for PLC1
1) Yoko-o T, et al.  (1993) The putative phosphoinositide-specific phospholipase C gene, PLC1, of the yeast Saccharomyces cerevisiae is important for cell growth. Proc Natl Acad Sci U S A 90(5):1804-8
2) Flick JS and Thorner J  (1998) An essential function of a phosphoinositide-specific phospholipase C is relieved by inhibition of a cyclin-dependent protein kinase in the yeast Saccharomyces cerevisiae. Genetics 148(1):33-47
3) Yoko-o T, et al.  (1995) Isolation and characterization of temperature-sensitive plc1 mutants of the yeast Saccharomyces cerevisiae. Mol Gen Genet 247(2):148-56
4) Galdieri L, et al.  (2013) Yeast Phospholipase C Is Required for Normal Acetyl-CoA Homeostasis and Global Histone Acetylation. J Biol Chem 288(39):27986-98
5) Flick JS and Thorner J  (1993) Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae. Mol Cell Biol 13(9):5861-76
6) York JD  (2006) Regulation of nuclear processes by inositol polyphosphates. Biochim Biophys Acta 1761(5-6):552-9
7) Ansari K, et al.  (1999) Phospholipase C binds to the receptor-like GPR1 protein and controls pseudohyphal differentiation in Saccharomyces cerevisiae. J Biol Chem 274(42):30052-8
8) DeLillo N, et al.  (2003) Genetic evidence for a role of phospholipase C at the budding yeast kinetochore. Mol Genet Genomics 269(2):261-70
9) Guha N, et al.  (2007) Plc1p is required for SAGA recruitment and derepression of Sko1p-regulated genes. Mol Biol Cell 18(7):2419-28
10) Demczuk A, et al.  (2008) Saccharomyces cerevisiae phospholipase C regulates transcription of Msn2p-dependent stress-responsive genes. Eukaryot Cell 7(6):967-79
11) Jun Y, et al.  (2004) Diacylglycerol and its formation by phospholipase C regulate Rab- and SNARE-dependent yeast vacuole fusion. J Biol Chem 279(51):53186-95
12) Rebecchi MJ and Pentyala SN  (2000) Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol Rev 80(4):1291-335