3VVW: NDP52 in complex with LC3C

Citation:
Abstract
Autophagy protects cellular homeostasis by capturing cytosolic components and invading pathogens for lysosomal degradation. Autophagy receptors target cargo to autophagy by binding ATG8 on autophagosomal membranes. The expansion of the ATG8 family in higher eukaryotes suggests that specific interactions with autophagy receptors facilitate differential cargo handling. However, selective interactors of ATG8 orthologs are unknown. Here we show that the selectivity of the autophagy receptor NDP52 for LC3C is crucial for innate immunity since cells lacking either protein cannot protect their cytoplasm against Salmonella. LC3C is required for antibacterial autophagy because in its absence the remaining ATG8 orthologs do not support efficient antibacterial autophagy. Structural analysis revealed that the selectivity of NDP52 for LC3C is conferred by a noncanonical LIR, in which lack of an aromatic residue is balanced by LC3C-specific interactions. Our report illustrates that specificity in the interaction between autophagy receptors and autophagy machinery is of functional importance to execute selective autophagy.
PDB ID: 3VVWDownload
MMDB ID: 107861
PDB Deposition Date: 2012/7/28
Updated in MMDB: 2018/06
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 3VVW: trimeric; determined by author and by software (PISA)
Molecular Components in 3VVW
Label Count Molecule
Proteins (3 molecules)
1
Calcium-binding and Coiled-coil Domain-containing Protein 2(Gene symbol: CALCOCO2)
Molecule annotation
2
Microtubule-associated Proteins 1a/1b Light Chain 3C(Gene symbol: MAP1LC3C)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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