BAIT

SLA2

END4, MOP2, L000001913, L000002421, YNL243W
Adaptor protein that links actin to clathrin and endocytosis; involved in membrane cytoskeleton assembly and cell polarization; present in the actin cortical patch of the emerging bud tip; dimer in vivo
GO Process (5)
GO Function (1)
GO Component (3)
Saccharomyces cerevisiae (S288c)
PREY

CDC55

TMR4, protein phosphatase 2A regulatory subunit CDC55, L000000282, S000029602, L000003191, YGL190C
Non-essential regulatory subunit B of protein phosphatase 2A (PP2A); localization to cytoplasm requires Zds1p and Zds2p and promotes mitotic entry; localization to nucleus prevents mitotic exit; required for correct nuclear division and chromosome segregation in meiosis; maintains nucleolar sequestration of Cdc14p during early meiosis; limits formation of PP2A-Rts1p holocomplexes to ensure timely dissolution of sister chromosome cohesion; homolog of mammalian B55
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

Stress-induced ceramide-activated protein phosphatase can compensate for loss of amphiphysin-like activity in Saccharomyces cerevisiae and functions to reinitiate endocytosis.

McCourt PC, Morgan JM, Nickels JT

Saccharomyces cerevisiae cells lacking the amphiphysin-like orthologs, Rvs161 or Rvs167, are unable to thrive under many stress conditions. Here we show cells lacking Rvs161 require Cdc55, the B subunit of the yeast ceramide-activated protein phosphatase, for viability under heat stress. By using specific rvs mutant alleles, we linked this lethal genetic interaction to loss of Rvs161 endocytic domain function. Recessive ... [more]

J. Biol. Chem. May. 01, 2009; 284(18);11930-41 [Pubmed: 19254955]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Curated By

  • BioGRID