A major barrier to understanding the mechanism of LRRK2 is the lack of structural information for the protein. In this journal club we are going to discuss the article The In Situ Structure of Parkinson’s Disease-Linked LRRK2 that tackled this barrier using correlative light and electron microscopy, in situ cryo-electron tomography, and subtomogram analysis.

The authors (Reika Watanabe et al.) reveal a 14-Å structure of LRRK2 and show its association with microtubules. The structure presented does not only provide insight to understand the pathogenic state of familial PD, but is also the first step towards designing improved LRRK2 kinase inhibitors. Are you interested in this topic? Don't miss the change to talk about it with our application specialists Dr. Caspar Jonker and Marit Smeets in our cryo-ET journal club!

You may prepare yourself by checking out the paper briefly before joining us. We also recommend you to read our technical page to learn more about cryo EM and cryo-ET in general.

This work is supported by the European SME2 grant № 879673 - Cryo-SECOM Workflow