It is well known that posttranslational modifications like phosphorylation and ubiquitination are involved in the regulation of the activity of proteins involved in autophagy and degradation of autophagic cargo proteins, respectively. However, little is known about how these modifications may regulate selective autophagy. The fact that the core Atg machinery is required for both nonselective and selective types of autophagy gives raise to the question of whether these two types of autophagy may compete for the same molecular machinery. Such a competition could be detrimental for the cells undergoing starvation and to avoid this, there might be a tight regulation of the expression level and/or activity of the proteins specifically involved the selective autophagy. It has recently been proposed that phosphorylation of autophagy receptors might be a general mechanism for the regulation of selective autophagy. Dikic and coworkers noted that several autophagy receptors contain conserved serine residues adjacent to their LIR motifs and indeed, the TANK binding kinase 1 (TBK1) was found to phosphorylate a serine residue close to the LIR motif of the autophagy receptor optineurin. This modification enhances the LC3 binding affinity of optineurin and promotes selective autophagy of ubiquitinated cytosolic Salmonella enterica [115] . In yeast, phosphorylation of Atg32, the autophagy receptor for mitophagy, by mitogen-activated protein kinases was found to be required for mitophagy [116, 117] .