The LC3 interactome at a glance

P Wild, DG McEwan, I Dikic - Journal of cell science, 2014 - journals.biologists.com
Journal of cell science, 2014journals.biologists.com
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 …
Abstract
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.
journals.biologists.com