BAIT
GGA1
RP1-37E16.3
golgi-associated, gamma adaptin ear containing, ARF binding protein 1
GO Process (1)
GO Function (1)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
ARF1
RP23-192P17.1
ADP-ribosylation factor 1
GO Process (18)
GO Function (6)
GO Component (9)
Gene Ontology Biological Process
- Golgi to transport vesicle transport [ISO]
- actin filament organization [ISO]
- cellular copper ion homeostasis [ISO]
- dendritic spine organization [ISO]
- long term synaptic depression [ISO]
- positive regulation of ER to Golgi vesicle-mediated transport [ISO]
- positive regulation of calcium ion-dependent exocytosis [ISO]
- positive regulation of dendritic spine development [ISO]
- positive regulation of endocytosis [ISO]
- positive regulation of late endosome to lysosome transport [ISO]
- positive regulation of protein secretion [ISO]
- positive regulation of sodium ion transmembrane transport [ISO]
- protein transport [TAS]
- regulation of Arp2/3 complex-mediated actin nucleation [ISO]
- regulation of receptor internalization [ISO]
- synaptic vesicle budding [ISO]
- very-low-density lipoprotein particle assembly [ISO]
- vesicle-mediated transport [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport.
GGAs are critical for trafficking soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes through interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to TGN membranes recruits its effector GGA by binding to the GAT domain, thus facilitating recognition of GGA for cargo-loaded receptors. Here we report the X-ray crystal structures of the human GGA1-GAT domain and ... [more]
Nat. Struct. Biol. May. 01, 2003; 10(5);386-93 [Pubmed: 12679809]
Throughput
- Low Throughput
Additional Notes
- N-terminal region of the human GGA1 GAT domain complexed with mouse ARF1 Q71L mutant protein lacking the N-terminal 17 residues
Curated By
- BioGRID