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The LC3 interactome at a glance
Philipp Wild, David G. McEwan, Ivan Dikic


Continuous synthesis of all cellular components requires their constant turnover in order for a cell to achieve homeostasis. To this end, eukaryotic cells are endowed with two degradation pathways – the ubiquitin-proteasome system and the lysosomal pathway. The latter pathway is partly fed by autophagy, which targets intracellular material in distinct vesicles, termed autophagosomes, to the lysosome. Central to this pathway is a set of key autophagy proteins, including the ubiquitin-like modifier Atg8, that orchestrate autophagosome initiation and biogenesis. In higher eukaryotes, the Atg8 family comprises six members known as the light chain 3 (LC3) or γ-aminobutyric acid (GABA)-receptor-associated protein (GABARAP) proteins. Considerable effort during the last 15 years to decipher the molecular mechanisms that govern autophagy has significantly advanced our understanding of the functioning of this protein family. In this Cell Science at a Glance article and the accompanying poster, we present the current LC3 protein interaction network, which has been and continues to be vital for gaining insight into the regulation of autophagy.


  • Competing interests

    The authors declare no competing interests.

  • Cell science at a glance

    A high-resolution version of the poster is available for downloading in the online version of this article at Individual poster panels are available as JPEG files at

  • Funding

    This work was supported by grants from Deutsche Forschungsgemeinschaft; the Cluster of Excellence ‘Macromolecular Complexes’ of the Goethe University Frankfurt; LOEWE Centrum for Gene and Cell therapy Frankfurt (to D.G.M and I.D.); and an European Research Council (ERC) grant agreement to I.D.

  • Supplementary material available online at

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