Microtubule nucleation from the nuclear envelope in fission yeast involves repurposing of nuclear export proteins for a non-export-related function, docking cytoplasmic proteins at nuclear pore complexes.

In response to proteotoxic stress, squamous cell carcinoma cells hijack the integrated stress response to promote recovery by bolstering protection of microtubule dynamics.

The microtubule organizing potential of the centrosome is inactivated in a stepwise process through phosphatase activity and mechanical disruption to remove an aging matrix of proteins.

In Caenorhabditis elegans, dendrites establish their unique microtubule polarity by localizing an organizing center behind the growing tip.

Myogenin promotes centrosome attenuation and establishes the nuclear envelope as the dominant microtubule organization center via the scaffold protein AKAP6, which is required for the recruitment of centrosomal proteins.

Molecular and cell biology analyses reveal novel roles of Polo-like kinases in establishing non-random segregation patterns of spindle-associated microtubule-organizing centers during mitosis, a phenomenon linked with replicative cell aging.

AKAP6 is a site-specific adaptor required and sufficient to anchor centrosomal proteins and golgi to the nuclear envelope and establishes a non-centrosomal microtubule organization center (ncMTOC).

In the absence of centrioles, components of pericentriolar material can self-organize into a single compact microtubule-organizing center through dynein-mediated transport of pericentrin-containing protein complexes if CAMSAP- and Golgi-mediated pathways of microtubule minus-end stabilization and anchoring are disabled.

CAMSAP2 co-condensates with αβ-tubulin to induce microtubule nucleation and growth, serving as a microtubule-organizing centre for non-centrosomal microtubules.

A mechanism for yeast centrosomes to differentiate the microtubule cytoskeleton.