WB, IHC, IPHost:
Species: Hu, Mu, Rt
Host: Rabbit Polyclonal
DLC8 protein bound efficiently to gephyrin in in vitro binding assays and colocalized with gephyrin during coexpression in HEK293 cells. The binding site for DLC8 was mapped to a fragment of 63 amino acids within the central linker domain of gephyrin. In hippocampal neurons, endogenous DLC8 protein was enriched at synaptic sites identified by synaptophysin and gephyrin immunostaining. Because DLC8 has been described as stoichiometric components of cytoplasmic dynein and myosin-Va complexes, results suggest that motor proteins are involved in the subcellular localization of gephyrin. DLC8 was identified as a transport molecule in the cytoplasm. DLC8 co-localizes with TRPS1 in dot-like structures in the cell nucleus. In an electrophoretic mobility shift assay it was shown that the interaction of DLC8 and TRPS1 lowers the binding of TRPS1 to the GATA consensus sequence. In addition DLC8 is able to suppress the transcriptional repression activity of TRPS1.
|Product By Gene ID
- Dynein light chain LC8-type 1
- Protein inhibitor of neuronal nitric oxide synthase
- dynein light chain 1, cytoplasmic
- dynein, cytoplasmic, light polypeptide 1
- cytoplasmic dynein light polypeptide
- dynein, light chain, LC8-type 1,8 kDa dynein light chain
Research Areas for PIN/DLC8
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