Post

Happy to share our work in @embojournal 👉 shorturl.at/zXNyn For decades, we’ve known cells dismantle & rebuild the nuclear envelope in sync with spindle poles. But why does this coordination matter? And how do pole material properties ensure error-free division? Follow this thread to know more 👇

When Aurora A is inactivated, we found that NuMA, a conserved spindle pole protein, undergoes a material state transition from dynamic to solid, and abnormally accumulates at the spindle poles. This abnormal “accumulation” causes NuMA segregated chromosomes/nuclei to bend around them.

NuMA accumulation at spindle poles depends on: • dynein/dynactin (trucks) • its coiled-coil domain (cranes), and • its ability to form multivalent cation-π interactions through its intrinsically disordered region (IDR) at the C-terminus (hooks in cyan).

We further show that dynamic-to-solid material state transition in the absence of Aurora A activity in anaphase is assisted by glutamine residues in its C-terminus IDR.