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Structural activation of Mad2 in the mitotic spindle checkpoint: the two-state Mad2 model versus the Mad2 template model Yu HJ Cell Biol 2006[Apr]; 173 (2): 153-7The inheritance of a normal assortment of chromosomes during each cell division relies on a cell-cycle surveillance system called the mitotic spindle checkpoint. The existence of sister chromatids that do not achieve proper bipolar attachment to the mitotic spindle in a cell activates this checkpoint, which inhibits the ubiquitin ligase activity of the anaphase-promoting complex or cyclosome (APC/C) and delays the onset of anaphase. The mitotic arrest deficiency 2 (Mad2) spindle checkpoint protein inhibits APC/C through binding to its mitotic-specific activator, Cdc20. Binding of Mad2 to Cdc20 involves a large conformational change of Mad2 and requires the Mad1-Mad2 interaction in vivo. Two related but distinct models of Mad1-assisted activation of Mad2, the "two-state Mad2" and the "Mad2 template" models, have been proposed. I review the recent structural, biochemical, and cell biological data on Mad2, discuss the differences between the two models, and propose experiments that test their key principles.|*Models, Biological[MESH]|Calcium-Binding Proteins/chemistry/*metabolism[MESH]|Cell Cycle Proteins/chemistry/*metabolism[MESH]|Mad2 Proteins[MESH]|Models, Molecular[MESH]|Nuclear Proteins/chemistry/metabolism[MESH]|Protein Conformation[MESH]|Repressor Proteins/chemistry/*metabolism[MESH]|Saccharomyces cerevisiae Proteins/chemistry/metabolism[MESH]|Spindle Apparatus[MESH] |
