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

CBK1

serine/threonine protein kinase CBK1, L000004609, YNL161W
Serine/threonine protein kinase of the the RAM signaling network; Ndr/LATS family member; binds regulatory subunit Mob2p; involved in regulation of cellular morphogenesis, polarized growth, and septum destruction; phosphorylation by Cbk1p regulates localization and activity of Ace2p transcription factor and Ssd1p translational repressor; Cbk1p activity is regulated by both phosphorylation and specific localization; relocalizes to cytoplasm upon DNA replication stress
Kinome Project (Sc)
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