Near the end of mitosis, p130 and p107 are dephosphorylated from their hyperphosphorylated state by the phosphatase PP2a. Inhibition of PP2a activity reduced promoter binding of some of the proteins of the DREAM complex in the subsequent G1 phase and de-repression of gene expression.
Other components have been shown to be phosphorylated for DREAM complex assembly to occur. Of these, LIN52 phosphorylation on its S28 residue is the most well-understood. Substitution of this serine to alanine led to reduced binding of the MuvB core to p130 and impaired the ability of cells to enter quiescence. This indicates that LIN52 S28 phosphorylation is required for proper association and function of the DREAM complex via binding with p130.  
One known regulator of phosphorylation of the S28 residue is the DYRK1A. The loss of this kinase leads to decreased phosphorylation of the S28 residue and association of p130 with MuvB. DYRK1A was also found to degrade cyclin D1, which would increase p21 levels – both of which contribute to cell cycle exit.
The DREAM complex was also shown to regulate cytokinesis through GAS2L3.