2020 Online Salon
TrkA Activation and the Auto-transphosphorylation Paradox
Project Details
- Entrant Name: Abrielle Cacciaglia
- Membership Type: Student Submission
- Address: Chicago, Illinois USA
- Client: University of Illinois at Chicago
- Copyright: 2020 Abrielle Cacciaglia
- Medium/software used: Print / VMD, Autodesk 3ds Max, Adobe Photoshop, Adobe Illustrator
- Final presentation format: Print poster
- Primary Audience: Undergraduate molecular biology students
Project Description
The binding of NGF to its high affinity receptor TrkA is a key regulator of neuronal differentiation and proliferation. The need for therapeutic interventions for neuropathologies such as Alzheimer’s disease makes this interaction an attractive area of study. The conformational modifications TrkA undergoes upon activation are integrally related to its contribution to downstream signaling pathways. TrkA also serves as a model for a common activation mechanism among receptor kinases: autophosphorylation. This piece visualizes TrkA’s role in neurotrophic signaling and its activation mechanism. By presenting the entirety of dimerized TrkA, the highly proximity-dependent process of trans-autophosphorylation can be better understood by viewers, who may believe it to be an improbable phenomenon. The highlighting of specific tyrosines which are phosphorylated during activation reinforces their differential roles, either as protein docking sites or modifiers of the catalytic site.
