Identification of essential residues for the C-terminal cleavage of the mammalian LC3: a lesson from yeast Atg8.
Atg8, a member of an evolutionarily conserved ubiquitin-like protein family, is involved in multiple membrane trafficking pathways including autophagy. In a recent study, we have identified two functional sites in the yeast Saccharomyces cerevisiae Atg8, one involving residues Tyr49 and Leu50, and the other--located on the opposite side of the molecule--residues Phe77 and Phe79. Here we extended our studies to the mammalian system and report that in LC3 residues Phe80 and Leu82, the equivalents of Phe77 and Phe79 in Atg8, are essential for its C-terminal cleavage. We propose that these residues are part of the Atg4 recognition site.
Fass
Ephraim
E
Departments of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel.
Amar
Nira
N
Elazar
Zvulun
Z
D020816:Amino Acid Motifs; D000818:Animals; D000071190:Autophagy-Related Protein 8 Family; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
C113757:ATG8 protein, S cerevisiae; D000071190:Autophagy-Related Protein 8 Family; C477012:MAP1LC3A protein, human; D008869:Microtubule-Associated Proteins; D029701:Saccharomyces cerevisiae Proteins