Specific glutamylation of some α-tubulin isotypes affects kinesin-1 localization and transport processes that depend on it, but their absence can speed up transport, possibly explaining why some large cells express α-tubulin isotypes that are not glutamylated.

Using linked TOG domains that each bind a curved conformation of αβ-tubulin, a microtubule polymerase catalyzes fast elongation by concentrating αβ-tubulin near the polymer end.

Biochemical, single molecule, cell and structural biology studies reveal an interaction between the kinesin-5 tail and motor domains regulating high-force production, which is critical for microtubule sliding motility.

A structure of the ciliary inner junction at 3.6 Å resolution permits atomic modeling of six inner junction proteins and their interactions with acetylated lysine 40 loops of alpha tubulins.

A buried mutation in αβ-tubulin reveals an allosteric response to GDP in the lattice that dictates microtubule catastrophe and shrinking.

LINKIN and three of its interactors-RUVBL1, RUVBL2, and α-tubulin-are required for cells to migrate together during organogenesis.

PARP-7 is a mono(ADP-ribosyl) transferase that directs an extensive ADP-ribosylated proteome to control microtubule stability, and regulate ovarian cancer cell growth and motility.

Soluble αβ-tubulin assembly is regulated by a cage-like molecular complex containing tubulin cofactors and Arl2.

Integrin- and ERK signaling stimulates mammary epithelial cell proliferation when extracellular collagen condenses, causing asymmetric growth of multicellular aggregates that is necessary for elongation during branching morphogenesis.

Cryo-EM studies of doublet microtubules from wild-type and acetylation mutants suggest that acetylation of K40 affects the lateral rotational angle between protofilaments, leading to changes in the structure and stability.