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Abstract

Autophagy is a mechanism of cellular upkeep by trafficking intracellular material to be degraded. Autophagy is known to be carried out by autophagy related proteins (Atg), yet the exact mechanism of how autophagy occurs has yet to be discovered. Due to its clinical relevance to conditions such as neurodegenerative and muscular diseases, a great deal of current research is being dedicated to further our understanding of how autophagy occurs. Atg11, a protein critical to a yeast’s ability to perform selective autophagy, may also hold many answers to selective autophagy within humans. Atg11 is a coiled-coil protein that interacts with Atg1, 9, 11, 20, 29, along with Ypt1 in selective autophagy. However, it is unknown how these interactions occur. Does Atg11 have multiple binding sites where it may bind to proteins simultaneously? Or does Atg11 have one competitive binding site where it can only bind with a single protein, and then release it before it may bind again? In this research we attempt to purify the binding portion of Atg11 so that it can be used to observe Atg11’s binding interactions with these proteins through a protein binding test mediated by a resin pulldown.

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