RALA
Gene Ontology Biological Process
- Ras protein signal transduction [TAS]
- actin cytoskeleton reorganization [IDA]
- chemotaxis [TAS]
- cytokinesis [IDA]
- membrane organization [TAS]
- membrane raft localization [IDA]
- neurotrophin TRK receptor signaling pathway [TAS]
- positive regulation of filopodium assembly [IDA]
- regulation of exocytosis [IDA]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ARF1
Gene Ontology Biological Process
- COPI coating of Golgi vesicle [TAS]
- GTP catabolic process [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class II [TAS]
- cellular copper ion homeostasis [IMP]
- dendritic spine organization [ISS]
- long term synaptic depression [ISS]
- membrane organization [TAS]
- phosphatidylinositol biosynthetic process [TAS]
- phospholipid metabolic process [TAS]
- post-Golgi vesicle-mediated transport [TAS]
- regulation of Arp2/3 complex-mediated actin nucleation [ISS]
- regulation of defense response to virus by virus [TAS]
- regulation of receptor internalization [ISS]
- retrograde vesicle-mediated transport, Golgi to ER [TAS]
- small molecule metabolic process [TAS]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA.
Phospholipase D1 (PLD1) is known to be activated by ADP-ribosylation factor 1 (ARF1). We report here that ARF1 co-immunoprecipitates with PLD1 and that the ARF1-dependent PLD activation is induced by the direct interaction between ARF1 and PLD1. We found that RalA, another member of the small GTP-binding proteins, synergistically enhances the ARF1-dependent PLD activity with an EC50 of about 30 ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID