SLC1, dynein light chain, L000003064, YDR424C
Cytoplasmic light chain dynein, microtubule motor protein; required for intracellular transport and cell division; involved in mitotic spindle positioning; forms complex with dynein intermediate chain Pac11p that promotes Dyn1p homodimerization, potentiates motor processivity; Dyn2p-Pac11p complex important for interaction of dynein motor complex with dynactin complex; acts as molecular glue to dimerize, stabilize Nup82-Nsp1-Nup159 complex module of cytoplasmic pore filaments
Saccharomyces cerevisiae (S288c)


F-actin-capping protein subunit beta, L000000215, YIL034C
Beta 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 (2)
GO Function (1)
GO Component (6)
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.


Mutations that enhance the cap2 null mutant phenotype in Saccharomyces cerevisiae affect the actin cytoskeleton, morphogenesis and pattern of growth.

Karpova TS, Lepetit MM, Cooper JA

Mutations conferring synthetic lethality in combination with null mutations in CAP2, the gene encoding the beta subunit of capping protein of Saccharomyces cerevisiae, were obtained in a colony color assay. Monogenic inheritance was found for four mutations, which were attributed to three genetic loci. One mutation, sac6-69, is in the gene encoding fimbrin, another actin-binding protein, which was expected because ... [more]

Genetics Nov. 01, 1993; 135(3);693-709 [Pubmed: 8293974]


  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Curated By

  • BioGRID