BAIT

TOR1

DRR1, phosphatidylinositol kinase-related protein kinase TOR1, L000002322, YJR066W
PIK-related protein kinase and rapamycin target; subunit of TORC1, a complex that controls growth in response to nutrients by regulating translation, transcription, ribosome biogenesis, nutrient transport and autophagy; involved in meiosis; TOR1 has a paralog, TOR2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

BEM2

IPL2, SUP9, TSL1, L000000168, YER155C
Rho GTPase activating protein (RhoGAP); involved in the control of cytoskeleton organization and cellular morphogenesis; required for bud emergence; potential GAP for Rho4p
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

Probing the membrane environment of the TOR kinases reveals functional interactions between TORC1, actin, and membrane trafficking in Saccharomyces cerevisiae.

Aronova S, Wedaman K, Anderson S, Yates J, Powers T

The TOR kinases are regulators of growth in eukaryotic cells that assemble into two distinct protein complexes, TORC1 and TORC2, where TORC1 is inhibited by the antibiotic rapamycin. Present models favor a view wherein TORC1 regulates cell mass accumulation, and TORC2 regulates spatial aspects of growth, including organization of the actin cytoskeleton. Here, we demonstrate that in yeast both TORC1 ... [more]

Mol. Biol. Cell Aug. 01, 2007; 18(8);2779-94 [Pubmed: 17507646]

Throughput

  • High Throughput

Ontology Terms

  • inviable (APO:0000112)

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TOR1 BEM2
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High-BioGRID
-

Curated By

  • BioGRID