Author

Jesse Smith

Date Approved

2018

Degree Type

Open Access Senior Honors Thesis

Department

Chemistry

First Advisor

Dr. Steven K. Backues

Second Advisor

Dr. Hedeel Evans

Third Advisor

Dr. Deborah Heyl-Clegg

Abstract

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

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