PAIP2 acts as a repressor in the regulation of translation initiation of polyadenylated mRNAs. Its inhibitory activity on translation is mediated through its interaction with PABPC1. PAIP2 displaces the interaction of PABPC1 with poly(A) RNA and competes with another protein, PAIP1, for binding to PABPC1. This displacement disrupts the cytoplasmic poly(A) ribonucleoprotein (RNP) structure organization, thereby inhibiting translation .
The regulation of mRNA translation is a critical process in cellular function, and PAIP2 plays a significant role in this regulation. By inhibiting the interaction between PABPC1 and poly(A) RNA, PAIP2 helps control the stability and translation of mRNAs. This regulation is essential for maintaining proper cellular function and responding to various cellular signals and stress conditions .
Research on PAIP2 has provided insights into its role in translational control and its potential implications in various biological processes and diseases. Studies have shown that PAIP2 can inhibit the translation of capped and polyadenylated mRNAs both in vitro and in vivo by displacing PABP from the poly(A) tail . This makes PAIP2 a potential target for therapeutic interventions in diseases where dysregulation of mRNA translation is a factor.
Mouse anti-human PAIP2 antibodies are used in research to study the expression and function of PAIP2 in human cells. These antibodies are generated by immunizing mice with human PAIP2 protein, and they can specifically bind to human PAIP2. This specificity allows researchers to investigate the role of PAIP2 in various cellular processes and to explore its potential as a therapeutic target.