3VVW

NDP52 in complex with LC3C

Summary for 3VVW

• Entry DOI: 10.2210/pdb3vvw/pdb
• Related: 3VVV
• Descriptor: Calcium-binding and coiled-coil domain-containing protein 2, Microtubule-associated proteins 1A/1B light chain 3C (3 entities in total)
• Functional Keywords: autophagy adaptor protein, protein transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 29410.63

Authors

Akutsu, M.,Muhlinen, N.V.,Randow, F.,Komander, D. (deposition date: 2012-07-28, release date: 2013-02-27, Last modification date: 2024-03-20)

Primary citation

Muhlinen, N.V.,Akutsu, M.,Ravenhill, B.J.,Foeglein, A.,Bloor, S.,Rutherford, T.J.,Freund, S.M.,Komander, D.,Randow, F.
LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy
Mol.Cell, 48:329-342, 2012

PubMed 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.

PubMed: 23022382
DOI: 10.1016/j.molcel.2012.08.024

Experimental method

X-RAY DIFFRACTION (2.5 Å)