Probing the Structure and Binding Partners of Asl to Elucidate its Role in Regulating the Centrosome (2014)

Undergraduates: Sarah Speed, Karen Plevock

Faculty Advisor: Kevin Slep
Department: Biology

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Centrosomes are highly regulated microtubule-organizing centers which serve as the primary site of microtubule nucleation in the cell. The fundamental ability of centrosomes to nucleate and anchor microtubules has important implications in many cellular processes such as organization of the microtubule cytoskeleton and regulation of cell division. Thus, tight regulation of centrosome composition and number is imperative in maintaining healthy cells. Our lab is interested in determining the structure and biochemical composition of key proteins involved in regulation of the centrosome. My current research focuses on the purification of the scaffolding protein Asterless (Asl) in two analogous systems, Drosophila melanogaster and Homo sapiens. By crystallizing Asl, structural determination through X-ray crystallography can be performed. Biochemical assays will also be conducted to determine the endogenous conformation of Asl. Previously, I have shown a novel localization of the third fragment of Asl to the centrosome. Asl has also been shown to recruit Plk4, the master regulator of centrosome duplication. Therefore, current experiments focus on finding the minimal domain of this third fragment that will localize to the centrosome in order to identify the possible region of interaction between Asl and Plk4. Through structural and biochemical assays of these key proteins, we hope to gain insight into the structural basis and the important regulation mechanisms of the centrosome.