BAIT

BZZ1

LSB7, YHR114W
SH3 domain protein implicated in regulating actin polymerization; able to recruit actin polymerization machinery through its SH3 domains; colocalizes with cortical actin patches and Las17p; interacts with type I myosins
GO Process (4)
GO Function (1)
GO Component (4)
Saccharomyces cerevisiae (S288c)
PREY

MYO3

myosin 3, L000002889, YKL129C
One of two type I myosins; localizes to actin cortical patches; deletion of MYO3 has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization; MYO3 has a paralog, MYO5, that arose from the whole genome duplication
GO Process (6)
GO Function (1)
GO Component (1)
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

Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro.

Soulard A, Lechler T, Spiridonov V, Shevchenko A, Shevchenko A, Li R, Winsor B

In Saccharomyces cerevisiae, the WASP (Wiskott-Aldrich syndrome protein) homologue Las17p (also called Bee1p) is an important component of cortical actin patches. Las17p is part of a high-molecular-weight protein complex that regulates Arp2/3 complex-dependent actin polymerization at the cell cortex and that includes the type I myosins Myo3p and Myo5p and verprolin (Vrp1p). To identify other factors implicated with this complex ... [more]

Mol. Cell. Biol. Nov. 01, 2002; 22(22);7889-906 [Pubmed: 12391157]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Additional Notes

  • MYO3/MYO5/BZZ1 triple mutants are synthetic lethal

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
BZZ1 MYO3
Two-hybrid
Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

High-BioGRID
-

Curated By

  • BioGRID