We and others previously identified the key structural domains of APC and Axin that are essential for destruction complex function and βcat destruction (e.g. Roberts et al., 2011).
The typical effects of such disasters include injury, death, infectious diseases outbreaks, large-scale population displacement, disruption of essential services, destruction of property and infrastructure, economic loss and psychological harm [ 2, 3].
Thus while APC is essential for destruction complex function, its role in the complex remained a mystery.
While current data suggest Axin polymerization and APC recruitment are essential for destruction complex function, previous microscopy provided only limited information about the internal structure of Axin APC complexes in vivo.
One mechanism involved was already known: the DIX domain of Axin polymerizes in a head-to-tail fashion, in which beta-sheet 2 of one DIX domain interacts with beta-sheet 4 of the next monomer, thus forming filaments, and this polymerization is essential for destruction complex function (Schwarz-Romond et al., 2007; Fiedler et al., 2011).
Strikingly, although other 20Rs are individually dispensable, both R2 and B are essential for the destruction complex to target βcat for destruction (Kohler et al., 2009; Roberts et al., 2011; Schneikert et al., 2014).
Specifically, the horizontal continuous reactor was suitable in view of ease of solid transfer, which is essential for complete destruction of PCBs and for full-scale applications.
Although Cdk1-Clb activity is essential for Swe1 destruction, activation of Cdc5 [5], Cdk1-Clb2 activity or interaction with Swe1 are dispensable for Swe1 degradation [6], [10].
Recently we have found that although Cdk1-Clb activity is essential for Swe1 destruction, the presence of Clb2 or its interaction with Swe1 is dispensable for Swe1 degradation [10].
The 26SP is also essential for the destruction of misfolded proteins that are generated by mistranslations and during stress.
