BAIT

OPY1

L000004016, YBR129C
Protein of unknown function; overproduction blocks cell cycle arrest in the presence of mating pheromone; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies
GO Process (0)
GO Function (0)
GO Component (2)

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

INP51

SJL1, phosphoinositide 5-phosphatase INP51, L000003319, YIL002C
Phosphatidylinositol 4,5-bisphosphate 5-phosphatase; synaptojanin-like protein with an N-terminal Sac1 domain, plays a role in phosphatidylinositol 4,5-bisphosphate homeostasis and in endocytosis; null mutation confers cold-tolerant growth
Kinome Project (Sc)
GO Process (1)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Publication

The dual PH domain protein Opy1 functions as a sensor and modulator of PtdIns(4,5)Pâ‚‚ synthesis.

Ling Y, Stefan CJ, Macgurn JA, Audhya A, Emr SD

Phosphatidylinositol-4,5-bisphosphate, PtdIns(4,5)P(2), is an essential signalling lipid that regulates key processes such as endocytosis, exocytosis, actin cytoskeletal organization and calcium signalling. Maintaining proper levels of PtdIns(4,5)P(2) at the plasma membrane (PM) is crucial for cell survival and growth. We show that the conserved PtdIns(4)P 5-kinase, Mss4, forms dynamic, oligomeric structures at the PM that we term PIK patches. The dynamic ... [more]

EMBO J. Jun. 29, 2012; 31(13);2882-94 [Pubmed: 22562153]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Additional Notes

  • inp51 inp52 opy1 triple null mutant

Curated By

  • BioGRID