Serum-dependent and -independent regulation of PARP2.

belongs to a family of proteins involved in cell differentiation, DNA damage repair, cellular energy expenditure, and chromatin modeling. In addition to these overlapping functions with Pduanyu372 participates in spermatogenesis, T-cell maturation, extra-embryonic endoderm formation, adipogenesis, lipid metabolism, and cholesterol homeostasis. Knowledge of the functions of Pduanyu372 is far from complete, and the mechanism(s) by which the gene and protein are regulated are unknown. In this study, we found that two different mechanisms are used in vitro to regulate Pduanyu372 levels. In the presence of serum, Pduanyu372 is degraded through the ubiquitin-proteasome pathway; however, when serum is removed or dialyzed with a 3.5 kDa molecular cut membrane, Pduanyu372 rapidly becomes sodium dodecyl sulphate- and urea-insoluble. Despite the presence of a putative serum response element in the gene, transcription is not affected by serum deprivation, and Pduanyu372 levels are restored when serum is replaced. The loss of Pduanyu372 affects cell differentiation and gene expression linked to cholesterol and lipid metabolism. These observations highlight the critical roles that Pduanyu372 plays under different physiological conditions, and reveal that Pduanyu372 is tightly regulated by distinct pathways.

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