BAIT

BRR6

YGL247W
Essential nuclear envelope integral membrane protein; required for nuclear envelope morphology, nuclear pore complex localization, nuclear export; exhibits synthetic lethal genetic interactions with genes involved in lipid metabolism
GO Process (3)
GO Function (0)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

ELO2

FEN1, GNS1, VBM2, fatty acid elongase ELO2, L000003126, L000000608, YCR034W
Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway; ELO2 has a paralog, ELO1, that arose from the whole genome duplication
GO Process (3)
GO Function (1)
GO Component (2)

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

Integral membrane proteins Brr6 and Apq12 link assembly of the nuclear pore complex to lipid homeostasis in the endoplasmic reticulum.

Hodge CA, Choudhary V, Wolyniak MJ, Scarcelli JJ, Schneiter R, Cole CN

Cells of Saccharomyces cerevisiae lacking Apq12, a nuclear envelope (NE)-endoplasmic reticulum (ER) integral membrane protein, are defective in assembly of nuclear pore complexes (NPCs), possibly because of defects in regulating membrane fluidity. We identified BRR6, which encodes an essential integral membrane protein of the NE-ER, as a dosage suppressor of apq12 Delta. Cells carrying the temperature-sensitive brr6-1 allele have been ... [more]

J. Cell. Sci. Jan. 01, 2010; 123(0);141-51 [Pubmed: 20016074]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Curated By

  • BioGRID