Identification of Essential Residues for the C-Terminal Cleavage of the Mammalian LC3: A Lesson from Yeast Atg8

Ephraim Fass, Nira Amar and Zvulun Elazar

volume 3 | issue 1

January/February 2007
Pages: 48 - 50

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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.

Addendum to:
Two Newly Identified Sites in the Ubiquitin-Like Protein Atg8 Are Essential for Autophagy
N. Amar, G. Lustig, Y. Ichimura, Y. Ohsumi and Z. Elazar
EMBO Rep 2006; 7:635-42

Authors

Ephraim Fass

Weizmann Institute of Science

Nira Amar

Weizmann Institute of Science

Zvulun Elazar

Department of Biological Chemistry; The Weizmann Institute of Science; Rehovot Israel

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link: