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Cell-cycle proteins are the proteins involved in regulation and maintenance of the cell cycle of eukaryotic cells. These include kinases and cyclins that regulate movement between the three phases of the cell cycle that leads to replication and division of a cell – these phases are interphase, mitosis and cytokinesis.
The formation of the mitotic checkpoint complex requires an intricate spatial coordination amongst the proteins Bub1, Mad1, Cdc20, and Mad2. Chen et al show that a structural flexibility in Mad1 plays an essential role in achieving this coordination.
The polarization of distinct scaffold-signaling hubs at opposite cell poles constitutes the basis of asymmetric cell division. Here, the authors show that phase separation serves as a general mechanism to regulate the assembly and dynamics of a new-pole scaffold-signaling hub.
Formation of the mitotic checkpoint complex (MCC) is catalysed by a phosphorylation-dependent scaffold. This work provides structural details of how a tripartite Mad1:Bub1:Cdc20 complex presents Cdc20 to Mad2, triggering open-to-closed conversion of Mad2 to assemble the MCC.
The natural product fucoxanthinol causes G1 arrest through decreasing the levels of ribosomal protein uS7, which directly binds and stabilises cyclin-dependent kinase 6.
Yamazaki et al. show that cell cycle-regulated changes in hyperphosphorylation of Ki-67 and NPM1 modulate alternating charge blocks in these proteins, which defines their propensity for liquid–liquid phase separation at chromatin.
The polyploidy of mammalian cardiomyocytes is a barrier to heart regeneration, but modification of the cardiomyocyte cell cycle can boost their regenerative potential.
The polyploidy of mammalian cardiomyocytes is a barrier to heart regeneration, but modification of the cardiomyocyte cell cycle can boost their regenerative potential.
