Polar Body Membrane Breakdown Occurs Independent of Macroautophagy in C. Elegans

<p>Failure to digest cell corpses can lead to lupus-like autoimmune disorders in mammals. To better understand if LC3-associated phagocytosis (LAP) drives cell corpse breakdown in phagolysosomes, we studied the clearance of the <em>C. elegans</em> polar body during embryonic development. ATG16L1 has separable roles in regulating LC3 recruitment during macroautophagy and LAP. We demonstrated that the ATG16L1 <em>C. elegans</em> orthologs, ATG-16.1 and ATG-16.2, function redundantly to promote polar body membrane breakdown. We also discovered that truncating the LAP-specific WD40 domain of ATG-16.2 unexpectedly disrupts autophagy. Furthermore, we confirmed that polar body membrane breakdown occurs independent of macroautophagy. We also showed that LC3 localizes to the phagolysosome independent of autophagosomes. Although these findings show macroautophagy is unlikely to be promoting polar body degradation, the mechanism by which LC3 is recruited to the polar body phagolysosome to promote cell corpse breakdown remains unknown.</p>

Name thesis:degree_name

M.S.

Level thesis:degree_level

Masters Thesis

Year dc:date.available

2023

Author dc:creator

• Kolli, Shruti

Contributors dc:contributor

• Ann Wehman
• J. Todd Blankenship
• Cedric Asensio

• ATG-16
• Cell corpse
• LC3-associated phagocytosis
• Macroautophagy
• Membrane breakdown
• Polar body
• Biochemistry, Biophysics, and Structural Biology
• Biology
• Cell and Developmental Biology
• Cell Biology
• Life Sciences
• Molecular Biology

Statement dc:rights

• <p>Copyright is held by the author. User is responsible for all copyright compliance.</p>

Language dc:language

English (eng)

Repository record dc:identifier

https://digitalcommons.du.edu/etd/2294

OAI identifier oai:identifier

oai:digitalcommons.du.edu:etd-3288