The maintenance of sister chromatid cohesion from S phase to the onset of 
anaphase relies on a small but evolutionarily conserved protein called Sororin. 
Sororin is a phosphoprotein and its dynamic localization and function are 
regulated by protein kinases, such as Cdk1/cyclin B and Erk2. The association of 
Sororin with chromatin requires cohesin to be preloaded to chromatin and 
modification of Smc3 during DNA replication. Sororin antagonizes the function of 
Wapl in cohesin releasing from S to G 2 phase and promotes cohesin release from 
sister chromatid arms in prophase via interaction with Plk1. This review focuses 
on progress of the identification and regulation of Sororin during cell cycle; 
role of post-translational modification on Sororin function; role of Sororin in 
the maintenance and resolution of sister chromatid cohesion; and finally 
discusses Sororin's emerging role in cancer and the potential issues that need 
be addressed in the future.