BAIT

LAA1

YJL207C
AP-1 accessory protein; colocalizes with clathrin to the late-Golgi apparatus; involved in TGN-endosome transport; physically interacts with AP-1; similar to the mammalian p200; may interact with ribosomes; YJL207C is a non-essential gene
GO Process (2)
GO Function (0)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

ERG11

CYP51, sterol 14-demethylase, L000000577, YHR007C
Lanosterol 14-alpha-demethylase; catalyzes the C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in the ergosterol biosynthesis pathway; member of the cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p
GO Process (1)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

Fast-evolving cofactors regulate the role of HEATR5 complexes in intra-Golgi trafficking.

Marmorale LJ, Jin H, Reidy TG, Palomino-Alonso B, Zysnarski CJ, Jordan-Javed F, Lahiri S, Duncan MC

The highly conserved HEATR5 proteins are best known for their roles in membrane traffic mediated by the adaptor protein complex-1 (AP1). HEATR5 proteins rely on fast-evolving cofactors to bind to AP1. However, how HEATR5 proteins interact with these cofactors is unknown. Here, we report that the budding yeast HEATR5 protein, Laa1, functions in two biochemically distinct complexes. These complexes are ... [more]

J Cell Biol Mar. 04, 2024; 223(3); [Pubmed: 38240799]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
LAA1 ERG11
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.2157BioGRID
2051859

Curated By

  • BioGRID