Dynein inhibition (bottom) prevents removal of Mad2 (red) from kinetochores.

The mitotic spindle checkpoint is a crucial cellular safety feature ensuring that both daughter cells will receive the correct number of chromosomes during cell division. Somehow the checkpoint is turned off only when the chromosomes are attached and aligned. Now on page 1159, Howell et al. show that a transport system using the cytoplasmic dynein/dynactin microtubule motor depletes several proteins from the outer domain of the kinetochore to inactivate the spindle checkpoint and allow mitosis to proceed.

Previously, Howell et al. found that the Mad2 checkpoint protein is transported from kinetochores to the spindle poles along spindle microtubules. The authors have now found that the microtubule motors CENP-E and cytoplasmic dynein, as well as the checkpoint-related proteins BubR1 and the 3F3/2 antigen, are also depleted from kinetochores and accumulate at the spindle poles. Inhibiting...

You do not currently have access to this content.