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Published in

American Association for the Advancement of Science, Science, 6524(371), p. 64-67, 2021

DOI: 10.1126/science.abc1424

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A tripartite mechanism catalyzes Mad2-Cdc20 assembly at unattached kinetochores

This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Data provided by SHERPA/RoMEO

Abstract

Checking fidelity in cell division Everything has to go right during cell division, so a checkpoint mechanism known as the spindle-assembly checkpoint prevents mitosis from proceeding unless the kinetochores that attach chromosomes to the spindle microtubules are properly engaged. Two papers now reveal the detailed molecular choreography that allows a single, unattached kinetochore to arrest cell division: Lara-Gonzalez et al. used a visual probe that tracks a specific form of one of the checkpoint complex proteins, and Piano et al. used a biochemical reconstitution of the checkpoint. Together, these studies reveal how protein interaction, spatial constraints, phosphorylation, and catalytic conversion of the protein Mad2 to its active form allow this all-important sensor to function. Science , this issue p. 64 , p. 67