Congratulations Moe!

Thank you, Irma, I completely agree. Beyond identifying the ciliary kinases, being able to define their specific substrates and phosphorylation sites would be an important next step. This has been especially challenging for DYRKs and large proteins like PCM1.

Many thanks to TUBITAK, @embo.org and @erc.europa.eu for funding and to Ebru Topcu for generating the DYRK3 interactome and Melis Arslanhan for its analysis and driving this story forward. We had great editorial experience at @commsbio.nature.com!

Through proximity mapping, loss-of-function and phenotypic rescue experiments, we found that DYRK kinases including DYRK3 ensure that the primary cilium assembles with proper length, stability and morphology.

A key turning point: we realized that GSK-626616, developed as a DYRK3 inhibitor, actually targets broader DYRK kinase activity. This led us to explore the roles of DYRKs, not just DYRK3, at the primary cilium.

This study represents many years of dedicated effort and fantastic collaboration from my amazing team members Efe, Selin, Ece, Ezgi, and Melis!

4- Disrupting satellite homeostasis impairs their roles in signaling.
Our work introduces new concepts and tools to investigate satellite biology. Huge thanks to @erc.europa.eu
SatelliteHomeostasis funding that allowed us to tackle this fundamental question comprehensively!

1- Satellites assemble via a hierarchical pathway initiated by PCM1 scaffold formation followed by sequential recruitment of other satellite proteins.
2- PCM1 scaffold forms through multimerization and phase separation.
3- Satellite granules have distinct internal subdomains.

After unraveling the functional importance of centriolar satellites for centrosomes and cilia, we shifted focus to understand their own intrinsic biology as standalone organelles, which led to exciting new findings.