AI Article Synopsis
- RanBPM is a novel binding protein that interacts with neurotrophin receptors, specifically p75NTR and the tyrosine kinase receptor TrkA, through its SPRY motif in the intracellular domain.
- The study utilized yeast two-hybrid, co-immunoprecipitation, and GST pull-down assays to confirm RanBPM's binding to TrkA and established that the interaction occurs in TrkA's tyrosine kinase domain.
- Overexpression of RanBPM was found to inhibit NFAT-dependent luciferase expression induced by NGF, indicating its potential role in regulating neurotrophin-mediated gene transcription and neuronal signaling.
Article Abstract
RanBPM as a novel binding protein can interact with neurotrophin receptor p75NTR and tyrosine kinase receptor Met which has a similar tyrosine kinase structure as receptor TrkA has. Whether RanBPM interacts with neurotrophin receptor TrkA has not been established to date. In this study, using yeast two-hybrid system, it was identified that RanBPM bound to the intracellular domain (ICD) of neurotrophin receptor TrkA through its SPRY motif. We confirmed the formation of complexes between RanBPM and TrkA by co-immunoprecipitation studies and GST pull-down assays. The region of TrkA interacted with the SPRY domain of RanBPM was located in its tyrosine kinase domain. Furthermore, coimmunoprecipitaiton revealed endogenous RanBPM and receptors TrkA did interact in several mammalian cell lines. It was found that the overexpression of RanBPM could inhibit NGF-induced increase of nuclear factor of activated T cells (NFAT) dependent luciferase expression through its interaction with receptor TrkA, and NFAT transcriptional activity plays an important role in neuronal signal transduction. These data suggested that RanBPM could participate in neurotrophin-mediated gene transcription and expression by its binding to TrkA.
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| http://dx.doi.org/10.1016/j.neulet.2006.06.059 | DOI Listing |
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