Work

C‐Terminal Tail Elongation Adds a New Dimension to the Tubulin Code

Year: 2026

Type: article

Abstract: Tubulin C-terminal tails undergo diverse post-translational modifications that regulate microtubule interactions with motors and severing enzymes. TTLL11, a member of the tubulin tyrosine ligase-like (TTLL) family, uniquely catalyzes glutamate addition to the terminal α-carboxyl group of both α- and β-primary tubulin tails. This linear C-terminal glutamylation enables the rescue of truncated tubulin variants and may support re-entry into the modification cycle. TTLL11 substrate specificity is determined by terminal residue identity rather than tubulin isotype. These findings expand the tubulin code and raise new questions about how linear and branched glutamylation are differentially recognized by microtubule-associated proteins.

Source: Cytoskeleton

DOI: 10.1002/cm.70088

Authors: Jana Campbell, Cyril Barinka

Institutions: Charles University, Czech Academy of Sciences, Institute of Biotechnology

Language: English

Topic: Microtubule and mitosis dynamics

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,920

Funders: Univerzita Karlova v Praze, Grantová Agentura, Univerzita Karlova, Grantová Agentura České Republiky, Akademie Věd České Republiky