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. 2001 Dec 24;155(7):1159–1172. doi: 10.1083/jcb.200105093

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Copyright © 2001, The Rockefeller University Press

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Figure 7. — Model of dynein/dynactin-driven poleward transport of kinetochore proteins along spindle microtubules, and the role of this transport in inactivation of the spindle checkpoint activity at kinetochores. (A) Mad2 + Mad2 complexes (blue oval) and other motor and checkpoint proteins (corona filament) assemble from cytoplasmic pools onto unattached kinetochores where the checkpoint proteins catalyze formation of Mad2-Cdc20 inhibitory complexes. (B) Dissociation of Mad2 and other outer domain components occurs either by direct exchange with cytoplasmic pools or through dynein/dynactin-interactions with non-kinetochore (nkMT) or kinetochore (kMT) microtubules. Motor and checkpoint protein complexes are transported poleward by dynein/dynactin where they dissociate into the cytoplasm. (C) Full kinetochore microtubule occupancy on metaphase-aligned chromosomes prevents association of outer domain components, thereby blocking formation of Mad2–Cdc20 inhibitory complexes and allowing for spindle checkpoint inactivation.