Editorial Open Access

Autophagy is a cellular process by which cellular components are engulfed inside distinct double-membrane structures (autophagosomes) and shuttled to the lysosomes for degradation. In addition to non-selective, bulk degradation of cytoplasmic contents, autophagosomes can selectively recycle unwanted organelles, remove protein aggregates, and eliminate invading viruses [1-4]. In recent years, the subject of the pathophysiological function of selective autophagy has received increasing attention. The adaptor proteins, including p62 (also known as sequestosome 1) and Nbr1 (neighbor of BRCA1 gene 1), have been revealed to be essential in mediating selective autophagy [2,5,6]. They function as autophagy receptors targeting ubiquitinated proteins to autophagosomes for degradation. Despite the difference in length and primary sequence, p62 and Nbr1 share a similar domain structure containing an N-terminal Phox/Bem1p (PB1) domain, an LC3-interacting region (LIR), an