Autophagy is an essential eukaryotic catabolic process that maintains cellular homeostasis by degrading unwanted cytoplasmic materials. Selective autophagy targets ubiquitinated substrates by attaching them to the phagophore through the mammalian autophagy related gene 8 (mAtg8). The mAtg8 family is split into two sub-families, there are three microtubule-associated protein 1A/1B-light chain 3 (LC3) and four gamma-aminobutyric acid receptor-associated protein (GABRAP) all of which are required for autophagosome maturation. Each mAtg8 has a ubiquitin-like β-grasp fold which is covalently attached to a phospholipid on the surface of the phagophore membrane, via a ubiquitin-like ligase cascade. Autophagy related proteins that posses the sequence motif: LC3 interacting region (LIR) can then interact with mAtg8.

Despite its importance of the mAtg8 family proteins during autophagy, there is currently a lack of biophysical data. We have examined the solution state of mAtg8 family proteins using multiangle light scattering (MALS) and anilytacal centrifugation (AUC) experiments and the thermal stability using differential scanning fluorimetry  (DSF).