A study on CLTA and its interaction with ATG8 proteins

Abstract

Autophagy is an essential cell mechanism for cell survival, where damaged organelles, misfolded proteins and invading pathogens can be broken down and the materials recycled. This process is dependent on double-membrane structures called autophagosomes engulfing and trafficking the contents to lysosomes for degradation. Proper formation of autophagosomes is therefore important in order to keep the cells healthy.

Clathrin-mediated endocytosis is a process where a clathrin mesh forms around invaginating vesicles to regulate and assists their formation and CLTA is an important part of this process. Therefore, the main aim of this thesis was to study CLTA and its interactions with ATG8 proteins.

The results of this study demonstrate how CLTA interacts with GABARAP though a conventional LIR-LDS interaction in vitro. An attempt was also made to determine where in the cell this interaction happens, but there were no conclusive evidence gathered. This must be further investigated in the future.