The Cvt pathway is a biosynthetic process mediating the transport of the three vacuolar hydrolases, aminopeptidase 1 (Ape1), aminopeptidase 4 (Ape4) and α-mannosidase (Ams1), and the Ty1 transposome into the vacuole [90, 91] . Ape1 is synthesized as a cytosolic precursor (prApe1), which multimerizes into the higher order Ape1 oligomer, to which Ape4, Ams1, and Ty1 associate to form the socalled Cvt complex, prior to being sequestered into a small autophagosome-like Cvt vesicle. Sequestration of the Cvt complex into Cvt vesicles is a multistep process, which requires the autophagy receptor Atg19, which facilitates binding to Atg8 at the PAS, as well as the adaptor protein Atg11 (Figure 2(a) ) [92] . Atg11 acts as a scaffold protein by directing the Cvt complex and Atg9 reservoirs translocation to the PAS in an actin-dependent way and then recruiting the Atg1/ULK complex [40, 93] . The PI3P-binding proteins Atg20, Atg21, and Atg24 are also required for the Cvt pathway [94, 95] , but their precise function remains to be elucidated. Interestingly, Atg11 overexpression was found to recruit more Atg8 and Atg9 to the PAS resulting in more Cvt vesicles. This observation indicates that Atg11 levels could regulate the rate of selective autophagy, and maybe also the size of the cargo-containing autophagosomes in yeast [90, 96] . Indeed, a series of studies has revealed that Atg11 is also involved in other types of selective autophagy such as mitophagy and pexophagy. However, the autophagy receptors involved in the different Atg11-dependent types Figure 2 : Representative selective autophagy. (a) The cytoplasm-to-vacuole targeting (Cvt) pathway. Ape1 is synthesized as a cytoplasmic precursor protein with a propeptide and rapidly oligomerizes into dodecamers that subsequently associate with each other to form a higher order complex. The autophagy receptor Atg19 directly binds to the complex and mediates the recruitment of another Cvt pathway cargo, Ams1, leading to the formation of the so-called Cvt complex. Atg19 also interacts with the autophagy adaptor Atg11 and this protein allows the transport of the Cvt complex to the site where the double-membrane vesicle will be generated. At this location, Atg11 tethers the Atg proteins essential for the Cvt vesicle formation and the direct binding of Atg19 to Atg8 permits the exclusive sequestration of the Cvt complex into the vesicle. (b) A model for p62 and NBR1 as autophagy receptors for ubiquitinated cargos. p62 and NBR1 bind with ubiquitinated cargos via their ubiquitin-associated (UBA) domain and this interaction triggers the aggregate formation through the oligomerization of p62 via its Phox and Bem1p (PB1) domain. Furthermore, p62 interacts with both autophagy-linked FYVE protein (ALFY), which serves to recruit Atg5 and to bind PI3P, and directly with LC3. This latter event appears to organize and activate the Atg machinery in close proximity of the ubiquitinated cargos, which allows to selectively sequester them in the autophagosomes in analogous to the Cvt pathway.