Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us Mol. Biol. Cell Jul (2006); 17(7):3304-17 Laa1p, a conserved AP-1 accessory protein important for AP-1 localization in yeast- Fernandez GE, Payne GS Department of Biological Chemistry, David Geffen School of Medicine at University of California, Los Angeles, Los Angeles, CA 90095, USA- 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- [PUBMED: 16687571] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.