Author

Carson Zois

Date Approved

2017

Degree Type

Open Access Senior Honors Thesis

Department

Chemistry

First Advisor

Dr. Steven K. Backues

Second Advisor

Dr. Hedeel Evans

Abstract

Autophagy is a physiological process for the degradation of internal cell components to promote cell survival. This process allows the cell to maintain homeostasis, recycle damaged cellular components and helps protect against disease. Autophagy can be selective or non-selective. Non-selective, or bulk, autophagy occurs during times of cellular starvation and results in non-specific degradation of cytoplasmic materials. Selective autophagy targets specific components within the cytoplasm for degradation, and is always active. In both forms of autophagy, components are degraded when a double-membraned structure, called the autophagosome, encapsulates the target cargo and is then recruited to the lysosome in mammalian cells, or the vacuole in yeast cells. There are approximately 30 proteins involved with the process of selective autophagy and one of the most understudied is Atg11. Atg11 has been shown to interact with a number of other autophagy proteins via its coiled-coil domains, 2 and 3. Thus, Atg11 is thought to be a central organizer of selective autophagy, but it is not known if Atg11 organizes its binding partners spatially, or temporally. We have expressed and purified our target portion of Atgl 1 as well as cleaved the GST-tag associated with Atgl 1 in its purified form. We have also shown that Atg11 self-interacts to form an oligomer in vitro.

Included in

Chemistry Commons

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