Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation.

ABSTRACT: Microtubules are cytoskeletal filaments that self-assemble from the protein tubulin, a heterodimer of α-tubulin and β-tubulin, and are important for cell mechanics, migration, and division. Much work has focused on how the nucleotide state of β-tubulin regulates the structure and dynamics of microtubules. In contrast, less is known about the structure and function of the C-terminal tails (CTTs) of α- and β-tubulin which are thought to freely protrude from the surface of the microtubule. To study the CTTs, we developed three different biosensors that bind the tyrosinated α-tubulin CTT (Y-αCTT) on the microtubule lattice. Surprisingly, live imaging of the probes indicates that the Y-αCTT is not accessible under normal cellular conditions. Lattice binding of the Y-αCTT probes can be increased

SUBMITTER: Hotta T 

PROVIDER: S-EPMC12485676 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature