This title appears in the Scientific Report : 2016 

Sequence-specific $^{1}$H, $^{15}$N, and $^{13}$C resonance assignments of the autophagy-related protein LC$_{3}$C
Krichel, Carsten
Weiergräber, Oliver H. / Pavlidou, Marina / Mohrlüder, Jeannine / Schwarten, Melanie / Willbold, Dieter / Neudecker, Philipp (Corresponding author)
Strukturbiochemie ; ICS-6
Biomolecular NMR assignments, 10 (2016) 1, S. 41-43
Dordrecht [u.a.] Springer Netherlands 2016
26280529
10.1007/s12104-015-9633-z
Journal Article
Engineering Cell Function
Please use the identifier: http://dx.doi.org/10.1007/s12104-015-9633-z in citations.
Autophagy is a versatile catabolic pathway for lysosomal degradation of cytoplasmic material. While the phenomenological and molecular characteristics of autophagic non-selective (bulk) decomposition have been investigated for decades, the focus of interest is increasingly shifting towards the selective mechanisms of autophagy. Both, selective as well as bulk autophagy critically depend on ubiquitin-like modifiers belonging to the Atg8 (autophagy-related 8) protein family. During evolution, Atg8 has diversified into eight different human genes. While all human homologues participate in the formation of autophagosomal membrane compartments, microtubule-associated protein light chain 3C (LC3C) additionally plays a unique role in selective autophagic clearance of intracellular pathogens (xenophagy), which relies on specific protein–protein recognition events mediated by conserved motifs. The sequence-specific 1H, 15N, and 13C resonance assignments presented here form the stepping stone to investigate the high-resolution structure and dynamics of LC3C and to delineate LC3C’s complex network of molecular interactions with the autophagic machinery by NMR spectroscopy.