Impact of Mex67 phosphorylation on Dbp5 binding

Publication Date

2026

Presentation Length

Poster/Gallery presentation

College

College of Sciences & Mathematics

Department

Biology, Department of

Student Level

Undergraduate

Faculty Mentor

Rebecca Adams, PhD

Presentation Type

Poster

Summary

mRNA export is an important step in gene expression, where mRNA moves from inside the nucleus and into the cytoplasm. Export of mRNA from the nucleus is dependent on the protein Mex67. This step allows DNA to be transcribed. Mex67 acts as crossing guard, carrying the mRNA through the nuclear pore complex (NPC). Once outside of the nucleus, the mRNA binds to Dbp5, and mex67 falls off, retreating inside of nucleus. This project aims to answer how dbp5 can remove mex67 from mRNA, but not other binding proteins. Phosphorylation adds negative charges to mex67. If mex67 is phosphorylated, how does that impact the ability of mex67 to unbind? Our hypothesis is that Dbp5 transiently binds to phosphorylated mex67. We will use a yeast 2 hybrid using phospho-mimetic and phospho-dead amino acid groups to test how phosphorylation impacts the interaction of mex67.

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