Using colocalization studies to explore potential interactions between the Drosophila proteins Kinesin, Dynactin and Eip63E

• In Event: Poster Presentation and Judging for: Biomedical; Cell & Molecular Biology; Chemistry & Biochemistry; Marine Science; Systematics & Evolutionary Biology.
  In Poster Session: Cell & Molecular Biology Poster session

Abstract

Dynactin is an important multi-subunit regulator of the microtubule motor dynein and regulates intracellular transport from fungi to humans. While important in most cells, dynactin function in the nervous system is of particular medical significance. The Glued subunit of dynactin is associated with multiple neurodegenerative diseases including distal spinal and bulbar muscular atrophy, Perry Syndrome and ALS. We previously performed a large-scale unbiased genetic screen identifying mutations in 250 genes whose partial loss-of-function either enhance or suppress the eye morphology defects in Drosophila Glued mutants. To focus on genes of likely relevance for motor disease, we further determined which of these mutations resemble Glued in yielding larval movement defects and axonal transport defects when combined with a mutation in kinesin-1. From this series of screens, we identified the kinase, Eip63E, which exhibits homology to a family of mammalian cyclin dependent kinases (Cdks) called PFTAIREs, whose function is currently poorly understood. Eip63E genetically interacts with both molecular motors, however it is unclear whether these proteins function together in the process of axonal transport. In order to address this question, we are preforming colocalization experiments to compare the cellular distributions of fluorescently tagged Eip63E, dynactin and kinesin proteins in Drosophila S2 cells.

Authors

• Kaitlin Beettner, Schreiner University

• Kara Miller, Schreiner University

• Susan Klinedinst, Schreiner University