Laura Ryder Tønnesen

• Presentation
• Research outputs

The aim of my Ph.D. project is to elucidate the biological role and molecular mechanisms of the two proteins pre-mRNA processing factor 39 (PRPF39) and tRNA selenocysteine 1 associated protein 1 (TRNAU1AP) assumed to play a role in alternative splicing. Alternative splicing is a key process in the regulation of cell- and tissue-specific expression patterns, affecting tissue identity and development.

My project is based on screen by our collaborator, which identified PRPF39 and TRNAU1AP, as positive regulators of the phosphorylation of the mitogen-activated protein kinase (MAPK) p38, together with a well-established upstream activator of p38 sterile-motif alpha and leucine zipper kinase (ZAK). We have shown that knocking out either PRPF39 or TRNAU1AP in human cells leads to the cells only expressing one of two protein isoforms of ZAK, suggesting that these two factors play a role in the splicing and regulation of ZAK expression. Additionally, I have found that PRPF39 and TRNAU1AP are interacting and that knockdown of one of the factors leads to an upregulation of the mRNA expression of the other. This suggests that the two factors may be a part of a common complex contributing to the splicing of the ZAK gene.

I am still in in the early stages of the project, being less than 1 year into my Ph.D., thus still a lot is to be investigated. In the near future, I will perform an interactome analysis to determine if TRNAU1AP and PRPF39 are interacting with parts of the spliceosome. Additionally, we hope to be able to identify the group of genes regulated by these two factors in addition to ZAK