{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kravec M"],"funding":["Agence Nationale de la Recherche (ANR)","Institut de convergence Q-life grant","Czech Academy of Sciences grant RVO","Funded by the European Union - Next Generation EU - National Institute for Cancer Research","Agence Nationale de la Recherche","European Regional Development Fund-Project","LabEx Cell&Scale grant","MEYS CR","Charles University Grant Agency","LabEx Cell&Scale grant","e-Infrastruktura CZ","Czech Science Foundation"],"pagination":["5635-5666"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11574253"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["43(22)"],"pubmed_abstract":["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 r"],"journal":["The EMBO journal"],"pubmed_title":["Carboxy-terminal polyglutamylation regulates signaling and phase separation of the Dishevelled protein."],"pmcid":["PMC11574253"],"funding_grant_id":["ANR-17-CONV-0005","INFRA LM2018140","86652036","LX22NPO5102","ANR-10-IDEX-0001-02","LM2018127","ANR-12-BSV2-0007","LM2018129","ANR-17-CE13-0021","CZ.02.1.01/0.0/0.0/18_046/0015974","GA22-06405S","GA22-25365S","1414120","ANR-11-LBX-0038","GA23-07149S","GX19-28347X"],"pubmed_authors":["Nedvedova J","Janke C","Bryja V","Tripsianes K","Gomoryova K","Sedo O","Zdrahal Z","Bologna S","Sulcova M","Kravec M","Zezula N","Harnos J","Cervenka I","Micka M","Barinka C","Potesil D","Sri Ganji R"],"additional_accession":[]},"is_claimable":false,"name":"Carboxy-terminal polyglutamylation regulates signaling and phase separation of the Dishevelled protein.","description":"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 r","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2026-06-01T20:29:40.092Z","creation":"2025-04-04T11:42:48.896Z"},"accession":"S-EPMC11574253","cross_references":{"pubmed":["39349846"],"doi":["10.1038/s44318-024-00254-7"]}}