Regulation of Capicua by ERK-Mediated Phosphorylation in Drosophila melanogaster 

Presenter

Roza Khalifa

Campus

UMass Boston

Sponsor

Jason Roush, Honors College, UMass Boston

Schedule

Session 3, 1:30 PM - 2:15 PM [Schedule by Time][Poster Grid for Time/Location]

Location

Poster Board A43, Campus Center Auditorium, Row 3 (A41-A60) [Poster Location Map]

Abstract

The RAS-MEK-ERK pathway is a kinase signaling cascade necessary for critical cellular processes such as cell proliferation, growth, and differentiation. Capicua (Cic) is a conserved transcriptional repressor that is controlled by the RAS-MEK-ERK pathway. Cic binds to DNA when repressing its target genes; its dysregulation is implicated in various human diseases such as cancer and neurodegeneration. Recent studies have suggested that the primary mode of Cic regulation involves phosphorylation by ERK which results in a decrease in Cic’s ability to repress target genes. Current models suggest that when Cic is phosphorylated, it dissociates from DNA and translocates from the nucleus to the cytoplasm, where it undergoes degradation. However, the precise mechanism is unclear. Previous work in our laboratory has identified several ERK dependent phosphorylation sites within the Cic protein. Cic phospho-mutants were constructed by substituting key serine and threonine amino acids with alanine. Sequencing results confirmed that we were successful in making various phospho-mutant constructs. Next steps will be to evaluate the effect of these mutations on Cic function in cultured cells and in vivo. Specifically, we will evaluate the stability of the mutant Cic protein isoforms. Our investigation will help advance our understanding of the regulation of Cic by ERK-mediated phosphorylation. 

Keywords

Developmental Biology, Kinase Signaling Pathway, Protein Function , Transcriptional Regulation

Research Area

Biological Organisms

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