This seminar was originally scheduled for 17 May but due to unforeseen circumstances has be postponed. The seminar will now take place on Tuesday 14 June 2022.
Dimeric conformation drives reelin's signaling pathway
Reelin is a secreted glycoprotein with well-characterized roles in the developing brain. This ~400 kDa protein forms a dimer and interacts with the very low-density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2) to initiate signal transduction. A mutant reelin monomer binds to its receptors but does not activate its signaling pathway.
In this talk, I’ll present data from my PhD work – including the steps I took to address this apparent decoupling of binding and signaling. I’ll describe the in-solution structure of reelin, derived using cryo-electron tomography and small angle X-ray scattering, and how a manipulated reelin heterodimer can still activate the reelin signaling pathway. Overall, I constructed a model of reelin signaling that is reliant on its stable, dimeric conformation. I’ll also share the high-resolution structure of reelin’s most C-terminal domain, which has recently been reported to bind to the co-receptor, neuropilin‑1 and affect the protein’s activity.
Zoom password: bioc
|Date||Tuesday, 14 June 2022|
|Time||12:00pm - 1:00pm|
|Audience||Undergraduate students,Postgraduate students,Staff|
Online and in-person
|Location||Biochemistry Seminar Room G.13 (BIG13), Dunedin and online via Zoom|
|Contact Name||Department of Biochemistry|