PRX
Gene Ontology Biological Process
Gene Ontology Molecular Function
DAG1
Gene Ontology Biological Process
- NLS-bearing protein import into nucleus [IDA]
- cytoskeletal anchoring at plasma membrane [IMP]
- extracellular matrix organization [TAS]
- membrane protein ectodomain proteolysis [IDA]
- microtubule anchoring [IMP]
- modulation by virus of host morphology or physiology [IDA]
- negative regulation of MAPK cascade [IMP]
- negative regulation of cell migration [IMP]
- negative regulation of protein kinase B signaling [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- basement membrane [IDA]
- contractile ring [IDA]
- cytoplasm [IDA]
- dystrophin-associated glycoprotein complex [IDA]
- extracellular region [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- filopodium [IDA]
- focal adhesion [IDA]
- integral component of membrane [IDA]
- lamellipodium [IDA]
- nucleoplasm [IDA]
- plasma membrane [IDA, TAS]
Affinity Capture-Western
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
Specific disruption of a schwann cell dystrophin-related protein complex in a demyelinating neuropathy.
Dystroglycan-dystrophin complexes are believed to have structural and signaling functions by linking extracellular matrix proteins to the cytoskeleton and cortical signaling molecules. Here we characterize a dystroglycan-dystrophin-related protein 2 (DRP2) complex at the surface of myelin-forming Schwann cells. The complex is clustered by the interaction of DRP2 with L-periaxin, a homodimeric PDZ domain-containing protein. In the absence of L-periaxin, DRP2 ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID