Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin
heterodimers. The primary sequence and structure of the tubulin proteins and, consequently …

Microtubule plus-end tracking proteins (+ TIPs) are a diverse group of evolutionarily
conserved cellular factors that accumulate at the ends of growing microtubules. They form …

Reversible detyrosination of α-tubulin is crucial to microtubule dynamics and functions, and
defects have been implicated in cancer, brain disorganization, and cardiomyopathies. The …

Microtubules create diverse arrays with specific cellular functions such as the mitotic spindle,
cilia, and bundles inside neurons. How microtubules are regulated to enable specific …

All microtubules are built from a basic α/β-tubulin building block, yet subpopulations of
microtubules can be differentially marked by a number of post-translational modifications …

In cells, stable microtubules (MTs) are covalently modified by a carboxypeptidase, which
removes the C-terminal Tyr residue of α-tubulin. The significance of this selective …

Tubulin tyrosine ligase (TTL) catalyzes the post-translational retyrosination of detyrosinated
α-tubulin. Despite the indispensable role of TTL in cell and organism development, its …

Tubulin-tyrosine ligase (TTL), the enzyme that catalyzes the addition of a C-terminal tyrosine
residue to α-tubulin in the tubulin tyrosination cycle, is involved in tumor progression and …

The microtubule cytoskeleton is crucial for the internal organization of eukaryotic cells.
Several microtubule-associated proteins link microtubules to subcellular structures. A …

Tubulin is subject to a special cycle of detyrosination/tyrosination in which the C-terminal
tyrosine of α-tubulin is cyclically removed by a carboxypeptidase and readded by a tubulin …