Presenter: Alani Estrella
Co-Presenters: Ken Prehoda, Matt Bailey
Presentation Type: Poster 60
Primary Research Area: Science
Major: Biochemistry
The accurate positioning and organization of molecules within animal cells is important for cell health. In fact, failure to correctly organize cell components is a key characteristic of metastatic cancers. Atypical protein kinase C (aPKC) is an enzyme that helps to properly localize a variety of cell components through a process called phosphorylation. The proteins that aPKC phosphorylates (known as substrates) have vastly different architectures. Although the phosphorylation of specific substrates has been researched intensely, such as Miranda (Mira) and Lethal giant larvae (Lgl), the general mechanism of aPKC substrate localization has remained elusive. Here, we sought to find a “polarity code,” or the molecular signature of substrates that aPKC organizes. To identify the polarity code, we developed a program that predicts novel aPKC substrates. Here we assessed the localization of these putative substrates to determine candidates for aPKC-regulated localization in fruit flies. We used a protein tagging technique that allows us to see protein expression and localization within brain cells. We observed the localization of three separate proteins: Alpha-Catenin, Dlp, and CG6454 to be cell-cycle dependent, suggesting possible aPKC-regulation. Future studies will focus on determining the mechanism through which these proteins are localized, whether aPKC is involved, and their roles in cell polarity. This study provides insight into how aPKC recognizes its substrates, and a further understanding of how animal cell components are organized by aPKC.