Informace o publikaci

Carboxy-terminal polyglutamylation regulates signaling and phase separation of the Dishevelled protein

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KRAVEC Marek ŠEDO Ondrej NEDVEDOVA Jana MICKA Miroslav ŠULCOVÁ Marie ZEZULA Nikodém GÖMÖRYOVÁ Kristína POTĚŠIL David GANJI Sri Ranjani BOLOGNA Sara ČERVENKA Igor ZDRÁHAL Zbyněk HARNOŠ Jakub TRIPSIANES Konstantinos JANKE Carsten BARINKA Cyril BRYJA Vítězslav

Rok publikování 2024
Druh Článek v odborném periodiku
Časopis / Zdroj EMBO Journal
Fakulta / Pracoviště MU

Lékařská fakulta

Citace
www https://www.embopress.org/doi/full/10.1038/s44318-024-00254-7
Doi http://dx.doi.org/10.1038/s44318-024-00254-7
Klíčová slova Dishevelled 3; Polyglutamylation; TTLL11; Noncanonical Wnt Signaling; Protein Condensates
Přiložené soubory
Popis Polyglutamylation is a reversible posttranslational modification that is catalyzed by enzymes of the tubulin tyrosine ligase-like (TTLL) family. Here, we found that TTLL11 generates a previously unknown type of polyglutamylation that is 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 Dishevelled 3 (DVL3), thereby changing the interactome of DVL3. Polyglutamylation increases the capacity of DVL3 to get phosphorylated, to undergo phase separation, and to act in the noncanonical Wnt pathway. Both carboxy-terminal polyglutamylation and the resulting reduction in phase separation capacity of DVL3 can be reverted by the deglutamylating enzyme CCP6, demonstrating a causal relationship between TTLL11-mediated polyglutamylation and phase separation. Thus, C-terminal polyglutamylation represents a new type of posttranslational modification, broadening the range of proteins that can be modified by polyglutamylation and providing the first evidence that polyglutamylation can modulate protein phase separation.
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