Characterizing the interaction between PDCD4 and eIF3 with respect to translation regulation
Sharma Khandiga, Divya
Lethbridge, Alta. : University of Lethbridge, Department of Chemistry and Biochemistry
Programmed cell death protein 4 (PDCD4) inhibits IRES-mediated translation of anti-apoptotic proteins such as XIAP. PDCD4 was shown to directly interact with the XIAP IRES element and inhibit translation initiation. Additionally, our lab reported that a eukaryotic initiation factor, eIF3 interacts with the XIAP IRES to facilitate ribosome recruitment. Interestingly, the activity of PDCD4 and eIF3 are regulated by common regulatory kinases called S6K1 and 2. Therefore, to investigate the possibility of interaction between PDCD4 and eIF3 as well as their co-regulation by S6K1 and 2, I have performed co-immunoprecipitation assays in glioblastoma and S6K double knockout MEFs. The results of in cellulo assays demonstrate RNA-independent PDCD4-eIF3 interactions. In addition, eIF3F, one of the 13 eIF3 subunits has been demonstrated to interact directly with PDCD4. This study suggests that the interaction of PDCD4 with eIF3F may have a role in regulating global and/or transcript-specific translation.
Genetic translation -- Research , Apoptosis -- Research , Tumor suppressor proteins -- Research , Dissertations, Academic , eIF3 , PDCD4 , PDCD4-eIF3 interaction , translation