BAIT

RVS167

amphiphysin, L000001789, YDR388W
Actin-associated protein with roles in endocytosis and exocytosis; interacts with Rvs161p to regulate actin cytoskeleton, endocytosis, and viability following starvation or osmotic stress; recruited to bud tips by Gyl1p and Gyp5p during polarized growth; homolog of mammalian amphiphysin
GO Process (4)
GO Function (2)
GO Component (4)
Saccharomyces cerevisiae (S288c)
PREY

INP52

SJL2, phosphatidylinositol-3-/phosphoinositide 5-phosphatase INP52, L000003985, YNL106C
Polyphosphatidylinositol phosphatase; dephosphorylates a number of phosphatidylinositol phosphates (PtdInsPs, PIPs) to PI; involved in endocytosis; hyperosmotic stress causes translocation to actin patches; synaptojanin-like protein with a Sac1 domain; INP52 has a paralog, INP53, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

Synthetic Growth Defect

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

Publication

Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and Rvs167 during Endocytosis.

Youn JY, Friesen H, Kishimoto T, Henne WM, Kurat CF, Ye W, Ceccarelli DF, Sicheri F, Kohlwein SD, McMahon HT, Andrews BJ

BAR domains are protein modules that bind to membranes and promote membrane curvature. One type of BAR domain, the N-BAR domain, contains an additional N-terminal amphipathic helix, which contributes to membrane-binding and bending activities. The only known N-BAR-domain proteins in the budding yeast Saccharomyces cerevisiae, Rvs161 and Rvs167, are required for endocytosis. We have explored the mechanism of N-BAR-domain function ... [more]

Mol. Biol. Cell Sep. 01, 2010; 21(17);3054-69 [Pubmed: 20610658]

Throughput

  • Low Throughput

Ontology Terms

  • resistance to chemicals (APO:0000087)
  • vegetative growth (APO:0000106)

Additional Notes

  • deletion of INP52 causes increased growth defects in an RVS161/RVS167 double mutant background
  • genetic complex

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
INP52 RVS167
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-4.0983BioGRID
580516
RVS167 INP52
Phenotypic Suppression
Phenotypic Suppression

A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.

Low-BioGRID
573577

Curated By

  • BioGRID