Atg8: an autophagy-related ubiquitin-like protein family |
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Authors: | Tomer Shpilka Hilla Weidberg Shmuel Pietrokovski Zvulun Elazar |
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Institution: | Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel. |
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Abstract: | Autophagy-related (Atg) proteins are eukaryotic factors participating in various stages of the autophagic process. Thus far
34 Atgs have been identified in yeast, including the key autophagic protein Atg8. The Atg8 gene family encodes ubiquitin-like
proteins that share a similar structure consisting of two amino-terminal α helices and a ubiquitin-like core. Atg8 family
members are expressed in various tissues, where they participate in multiple cellular processes, such as intracellular membrane
trafficking and autophagy. Their role in autophagy has been intensively studied. Atg8 proteins undergo a unique ubiquitin-like
conjugation to phosphatidylethanolamine on the autophagic membrane, a process essential for autophagosome formation. Whereas
yeast has a single Atg8 gene, many other eukaryotes contain multiple Atg8 orthologs. Atg8 genes of multicellular animals can
be divided, by sequence similarities, into three subfamilies: microtubule-associated protein 1 light chain 3 (MAP1LC3 or LC3),
γ-aminobutyric acid receptor-associated protein (GABARAP) and Golgi-associated ATPase enhancer of 16 kDa (GATE-16), which
are present in sponges, cnidarians (such as sea anemones, corals and hydras) and bilateral animals. Although genes from all
three subfamilies are found in vertebrates, some invertebrate lineages have lost the genes from one or two subfamilies. The
amino terminus of Atg8 proteins varies between the subfamilies and has a regulatory role in their various functions. Here
we discuss the evolution of Atg8 proteins and summarize the current view of their function in intracellular trafficking and
autophagy from a structural perspective. |
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