The autophagy receptors p62 and neighbour of BRCA1 gene (NBR1) bind both ubiquitinated protein aggregates through an ubiquitin-associated (UBA) domain and to LC3 via their LIR motifs and, thereby, promote the specific autophagic degradation of ubiquitinated proteins (Figure 2(b) ) [81, 82, 100, 103, 104] . NBR1 and p62 also contain an Nterminal Phox and Bem1p (PB1) domain through which they can oligomerize, or interact with other PB1-containing binding partners [83] . In addition to being a cargo receptor for protein aggregates, p62 has been implicated in autophagic degradation of other ubiquitinated substrates such as intracellular bacteria [105] , viral capsid proteins [106] , the midbody remnant formed after cytokinesis [107] , peroxisomes [108, 109] , damaged mitochondria [110, 111] , and bacteriocidal precursor proteins [112] . The PB1 domain was recently found to be required for p62 to localize to the autophagosome formation site adjacent to the ER [113] , suggesting that it could target ubiquitinated cargo to the site of autophagosome formation or alternatively promote the assembly of the Atg machinery at this location.