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Scaffolding the expansion of autophagosomes
#MMPMID24963637
Kaufmann A
; Wollert T
Autophagy
2014[Jul]; 10
(7
): 1343-5
PMID24963637
show ga
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.
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