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

RPL15A

RPL10A, ribosomal 60S subunit protein L15A, L15e, rp15R, YL10, L15A, L13A, L000002705, L000001710, YLR029C
Ribosomal 60S subunit protein L15A; binds to 5.8 S rRNA; homologous to mammalian ribosomal protein L15, no bacterial homolog; RPL15A has a paralog, RPL15B, that arose from the whole genome duplication
GO Process (1)
GO Function (2)
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

Curated By

  • BioGRID