CDH2
Gene Ontology Biological Process
- adherens junction organization [TAS]
- cell adhesion [TAS]
- cell junction assembly [TAS]
- cell-cell adhesion mediated by cadherin [ISS]
- cell-cell junction organization [TAS]
- glial cell differentiation [ISS]
- muscle cell differentiation [TAS]
- neuronal stem cell maintenance [ISS]
- positive regulation of muscle cell differentiation [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
GNA13
Gene Ontology Biological Process
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
Interaction of Galpha 12 and Galpha 13 with the cytoplasmic domain of cadherin provides a mechanism for beta -catenin release.
The G12 subfamily of heterotrimeric G proteins, comprised of the alpha-subunits Galpha12 and Galpha13, has been implicated as a signaling component in cellular processes ranging from cytoskeletal changes to cell growth and oncogenesis. In an attempt to elucidate specific roles of this subfamily in cell regulation, we sought to identify molecular targets of Galpha12. Here we show a specific interaction ... [more]
Throughput
- Low Throughput
Additional Notes
- Whereas the cadherin-14 tail bound similar amounts of GTPS-bound and GDP-bound G12, the E-cadherin and N-cadherin tails bound G12 in an activation-specific manner;heterotrimeric form of G12 does not bind to the cadherin cytoplasmic domain;Galpha12 or Galp
Curated By
- BioGRID