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Ubiquitin-like proteins fall into two classes: the first class, ubiquitin-like modifiers (UBLs) function as modifiers in a manner analogous to that of ubiquitin. Examples of UBLs are SUMO, Rub1 (also called Nedd8), Apg8 and Apg12. Proteins of the second class include parkin, RAD23 and DSK2, are designated ubiquitin-domain proteins (UDPs). These proteins contain domains that are related to ubiquitin but are otherwise unrelated to each other. In contrast to UBLs, UDPs are not conjugated to other proteins. Apg8 is required for autophagy (intracellular bulk protein degradation) in yeast. Starved yeast cells take up their own cytoplasm into vacuoles through autophagic bodies. Autophagic bodies form a double-membraned structure called the autophagosome, which subsequently fuses with the vacuole/lysosome. This process similar in mammals. Two sets of genes, APG and AUT, have been identified with this process, and are responsible for two ubiquitin-like systems Apg12 and Apg8, respectively. Apg12 is synthesized in its mature form and seems to have one target, Apg5. Almost all Apg12 molecules are conjugated with Apg5.
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