Jesse Smith

Date Approved


Degree Type

Open Access Senior Honors Thesis

Department or School


First Advisor

Dr. Steven K. Backues

Second Advisor

Dr. Hedeel Evans

Third Advisor

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.

Included in

Chemistry Commons