Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2023.07.28.550915v1?rss=1

Authors: Kravec, M., Sedo, O., Nedvedova, J., Micka, M., Sulcova, M., Gomoryova, K., Potesil, D., Ganji, R. S., Cervenka, I., Zdrahal, Z., Harnos, J., Tripsianes, K., Janke, C., Barinka, C., Bryja, V.

Abstract:
Polyglutamylation is a reversible post-translational modification that is catalyzed by enzymes from the tubulin tyrosine ligase-like (TTLL) family. Here, we found that TTLL11 generates a previously unknown type of polyglutamylation initiated by the addition of a glutamate residue to the free C-terminal carboxyl group of a substrate protein. TTLL11 efficiently polyglutamylates the Wnt signaling protein Disheveled 3 (DVL3), thereby changing the interactome of DVL3, as well as increases its capacity to get phosphorylated, to undergo liquid-liquid phase separation (LLPS) and to act in the non-canonical Wnt pathway. Both carboxyterminal polyglutamylation and the resulting reduction in LLPS capacity of DVL3 were reverted by the deglutamylating enzyme CCP6, which demonstrates the causal relationship between TTLL11-mediated polyglutamylation and LLPS. We thus discovered a novel type of posttranslational modification, which significantly broadens the range of proteins that can be modified by polyglutamylation and provide first evidence that polyglutamylation can act as a regulator of protein LLPS.

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