Mathias Cobbaut

Capture, mutual inhibition and release mechanism for aPKC–Par6 and its multisite polarity substrate Lgl - Nature Structural & Molecular Biology Combining structural, biochemical, cellular and in vivo assays, the authors uncover the mechanism for capture and multisite phosphorylation of lethal (2) giant larvae by the atypical protein kinase C ...

Excited to share our latest publication 🚨

We reveal insights into how a key protein kinase orchestrates cell polarity, uncovering unexpected molecular behaviours that shape this essential biological process!

Great work from everyone involved at the @crick.ac.uk and @polarityi3s.bsky.social

Capture, mutual inhibition and release mechanism for aPKC–Par6 and its multisite polarity substrate Lgl - Nature Structural & Molecular Biology Combining structural, biochemical, cellular and in vivo assays, the authors uncover the mechanism for capture and multisite phosphorylation of lethal (2) giant larvae by the atypical protein kinase C ...

Excited to share our latest publication 🚨

We reveal insights into how a key protein kinase orchestrates cell polarity, uncovering unexpected molecular behaviours that shape this essential biological process!

Great work from everyone involved at the @crick.ac.uk and @polarityi3s.bsky.social

I sometimes forget how flexible proteins are. It becomes really apparent when you use NMR states for an animation. That poor cofactor is getting pushed around a lot 😅

#sciart #blender3d #biocatalysis

Hi everyone 👋! Introducing myself here: I study protein kinases in all their remarkable complexity, venturing far beyond simple phosphotransfer, hoping to learn how we can better target the ones that misbehave! 🦹‍♂️

and I'm here for blue skies (and bench space?)