Autophagy receptors are defined as proteins being able to interact directly with both the autophagosome cargo and the Atg8/LC3 family members through a specific (WxxL) sequence [80] , commonly referred to as the LC3-interacting region (LIR) motif [81] or the LC3 recognition sequences (LRS) [82] . Based on comparison of LIR domains from more than 20 autophagy receptors it was found that the LIR consensus motif is an eight amino acids long sequence that can be written D/E-D/E-D/E-W/F/Y-X-X-L/I/V. Although not an absolute requirement, usually there is at least one acidic residue upstream of the W-site. The terminal L-site is occupied by a hydrophobic residue, either L, I, or V [83] . The LIR motifs of several autophagy receptors have been found to interact both with LC3 and GABARAP family members in vitro, but whether this reflects a physiological interaction remains to be clarified in most cases. It should be pointed out that not all LIR-containing proteins are autophagy cargo receptors. Some LIR-containing proteins, like Atg3 and Atg4B, are recruited to autophagic membranes to perform their function in autophagosome formation [84, 85] , whereas others like FYVE and coiled-coil domain-containing protein 1 (FYCO1) interact with LC3 to facilitate autophagosome transport and maturation [86] . Others might use an LIR motif to become degraded, like Dishevelled, an adaptor protein in the Wnt signalling pathway [87] . The adaptor proteins are less well-described, but seem to interact with autophagy receptors and work as scaffold proteins recruiting and assembling the Atg machinery required to generate autophagosomes around the cargo targeted to degradation. Examples of autophagy adaptors are Atg11 and ALFY [88, 89] .