ArticleMolecular biology of the cell2006
Laa1p, a conserved AP-1 accessory protein important for AP-1 localization in yeast.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Fast-evolving cofactors regulate the role of HEATR5 complexes in intra-Golgi trafficking.The Journal of cell biology · 2024Article
- HEATR5B associates with dynein-dynactin and promotes motility of AP1-bound endosomal membranes.The EMBO journal · 2023Article
- Two functionally distinct HEATR5 protein complexes are defined by fast-evolving co-factors in yeast.bioRxiv : the preprint server for biology · 2023Article
- New directions for the clathrin adaptor AP-1 in cell biology and human disease.Current opinion in cell biology · 2022Review
- Arf1 directly recruits the Pik1-Frq1 PI4K complex to regulate the final stages of Golgi maturation.Molecular biology of the cell · 2021Article
- Clathrin Adaptor Complex-interacting Protein Irc6 Functions through the Conserved C-Terminal Domain.Scientific reports · 2019Article
- Adaptor protein complex-1 (AP-1) is recruited by the HEATR5 protein Laa1 and its co-factor Laa2 in yeast.The Journal of biological chemistry · 2019Article
- Energy metabolism regulates clathrin adaptors at the trans-Golgi network and endosomes.Molecular biology of the cell · 2013Article
- Sip1, an AP-1 accessory protein in fission yeast, is required for localization of Rho3 GTPase.PloS one · 2013Article
- Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins.Molecular biology of the cell · 2012Article
- Phosphoinositide-mediated clathrin adaptor progression at the trans-Golgi network.Nature cell biology · 2012Article
- Sip1, a conserved AP-1 accessory protein, is important for Golgi/endosome trafficking in fission yeast.PloS one · 2012Article
- Glucose regulates clathrin adaptors at the trans-Golgi network and endosomes.Molecular biology of the cell · 2011Article
- Epsin N-terminal homology domains bind on opposite sides of two SNAREs.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Alpha-arrestins Aly1 and Aly2 regulate intracellular trafficking in response to nutrient signaling.Molecular biology of the cell · 2010Article
- Functional characterization of protein-sorting machineries at the trans-Golgi network in Drosophila melanogaster.Journal of cell science · 2010Article
- Identification of a conserved F-box protein 6 interactor essential for endocytosis and cytokinesis in fission yeast.The Biochemical journal · 2009Article
- Lessons from fungal F-box proteins.Eukaryotic cell · 2009Review
- Distinct roles for TGN/endosome epsin-like adaptors Ent3p and Ent5p.Molecular biology of the cell · 2006Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
AP-1 and Gga adaptors participate in clathrin-mediated protein transport between the trans-Golgi network and endosomes. Both adaptors contain homologous domains that act to recruit accessory proteins involved in clathrin-coated vesicle formation, but the spectrum of known adaptor-binding partners is limited. This study describes an evolutionarily conserved protein of Saccharomyces cerevisiae, Laa1p (Yjl207cp), that interacts and functions specifically with AP-1. Deletion of LAA1, when combined with a conditional mutation in clathrin heavy chain or deletion of GGA genes, accentuated growth defects and increased disruption of clathrin-dependent alpha-factor maturation and transport of carboxypeptidase Y to the vacuole. In contrast, such genetic interactions were not observed between deletions of LAA1 and AP-1 subunit genes. Laa1p preferentially interacted with AP-1 compared with Gga proteins by glutathione S-transferase-fusion affinity binding and coimmunoprecipitations. Localization of AP-1 and Laa1p, but not Gga proteins, was highly sensitive to brefeldin A, an inhibitor of ADP-ribosylation factor (Arf) activation. Importantly, deletion of LAA1 caused mislocalization of AP-1, especially in cells at high density (postdiauxic shift), but it did not affect Gga protein distribution. Our results identify Laa1p as a new determinant of AP-1 localization, suggesting a model in which Laa1p and Arf cooperate to direct stable association of AP-1 with appropriate intracellular membranes.
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