BAIT

SAC6

ABP67, fimbrin, L000001793, YDR129C
Fimbrin, actin-bundling protein; cooperates with Scp1p (calponin/transgelin) in the organization and maintenance of the actin cytoskeleton; relocalizes from plasma membrane to cytoplasm upon DNA replication stress
GO Process (1)
GO Function (2)
GO Component (6)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

CAP1

L000000214, YKL007W
Alpha subunit of the capping protein heterodimer (Cap1p and Cap2p); capping protein (CP) binds to the barbed ends of actin filaments preventing further polymerization; localized predominantly to cortical actin patches; protein increases in abundance and relocalizes from bud neck to plasma membrane upon DNA replication stress
GO Process (1)
GO Function (1)
GO Component (7)

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

Unexpected combinations of null mutations in genes encoding the actin cytoskeleton are lethal in yeast.

Adams AE, Cooper JA, Drubin DG

To understand the role of the actin cytoskeleton in cell physiology, and how actin-binding proteins regulate the actin cytoskeleton in vivo, we and others previously identified actin-binding proteins in Saccharomyces cerevisiae and studied the effect of null mutations in the genes for these proteins. A null mutation of the actin gene (ACT1) is lethal, but null mutations in the tropomyosin ... [more]

Mol. Biol. Cell May. 01, 1993; 4(5);459-68 [Pubmed: 8334302]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Additional Notes

  • in cap2 background

Curated By

  • BioGRID