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Journal Article

Scaffolding the expansion of autophagosomes

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Kaufmann,  Anna
Wollert, Thomas / Molecular Membrane and Organelle Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Wollert,  Thomas
Wollert, Thomas / Molecular Membrane and Organelle Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Kaufmann, A., & Wollert, T. (2014). Scaffolding the expansion of autophagosomes. AUTOPHAGY, 10(7), 1343-1345. doi:10.4161/auto.28980.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0023-C3F9-3
Abstract
The conjugation of the small ubiquitin (Ub)-like protein Atg8 to autophagic membranes is a key step during the expansion of phagophores. This reaction is driven by 2 interconnected Ub-like conjugation systems. The second system conjugates the Ub-like protein Atg12 to Atg5. The resulting conjugate catalyzes the covalent attachment of Atg8 to membranes. Atg12-Atg5, however, constitutively associates with the functionally less well-characterized coiled-coil protein Atg16. By reconstituting the conjugation of Atg8 to membranes in vitro, we showed that after Atg8 has been attached to phosphatidylethanolamine (PE), it recruits Atg12-Atg5 to membranes by recognizing a noncanonical Atg8-interacting motif (AIM) within Atg12. Atg16 crosslinks Atg8-PE-Atg12-Atg5 complexes to form a continuous 2-dimensional membrane scaffold with meshwork-like architecture. Apparently, scaffold formation is required to generate productive autophagosomes and to deliver autophagic cargo to the vacuole in vivo.