Open Access Senior Honors Thesis
Dr. Steven K. Backues
Dr. Hedeel Evans
Dr. Deborah Heyl-Clegg
Autophagy is a mechanism of intracellular degradation within eukaryotes. Because of its aid to a cells longevity, autophagy is believed to be important for the prevention of neurodegenerative diseases. Autophagy related protein 11 (Atg11) is a coiled-coil scaffolding protein required for selective autophagy in yeast. Atg11 is known to interact with Atg1, Atg20, and Atg29, in addition to connecting cargo molecules prApel -Atg19 to the phagophore assembly site. In addition to its many functions within yeast autophagy, Atg11 has two human homologs: Huntingtin protein and FIP200. This homology encourages us to gain a further understanding of Atg11's binding sites. In this study we show that making two mutations within the coiled-coil domain 2 of Atg11, 1562E/Y565E, causes it to lose its ability to interact with Atg1.
Smith, Jesse, "Determining Atg11's Binding Interactions Using a Yeast Two Hybrid System and Directed Mutagenesis" (2018). Senior Honors Theses. 576.