The article reviews the mechanisms and significance of selective autophagy in mammalian cells, focusing on the roles of autophagic adapters p62 and NBR1. Selective autophagy is a more targeted form of autophagy that degrades specific substrates, such as misfolded proteins, protein aggregates, mitochondria, and invading bacteria. The process involves the interaction between autophagic adapters and the autophagosomal marker protein LC3, mediated by a LIR (LC3-interacting region) motif. This interaction, along with the ability to polymerize or aggregate and specific substrate recognition, is essential for efficient selective autophagy. The article discusses the degradation of various cellular components, including misfolded proteins, p62 bodies, aggresomes, mitochondria, and bacteria, and highlights the emerging role of selective autophagy in regulating cell signaling, oxidative stress responses, tumorigenesis, and innate immunity. The importance of p62 and NBR1 as cargo receptors for ubiquitinated substrates is emphasized, along with their involvement in bone remodeling and T-cell activation. The LIR-ATG8 (LC3/GABARAP) interaction is described in detail, including the structural basis and functional significance. The article also explores the hypothesis that p62 and NBR1 act as adapters for the selective autophagy of ubiquitinated substrates, and discusses the formation and degradation of p62 bodies, aggresomes, and other specialized structures. The role of p62 in the constitutive and stress-induced autophagy of misfolded proteins is highlighted, along with the consequences of inefficient autophagic degradation leading to the accumulation of ubiquitinated aggregates. The selective autophagy of aggregated protein substrates, such as aggresomes, and the selective removal of damaged mitochondria (mitophagy) are also covered, emphasizing the importance of specific adapters and signaling pathways in these processes.The article reviews the mechanisms and significance of selective autophagy in mammalian cells, focusing on the roles of autophagic adapters p62 and NBR1. Selective autophagy is a more targeted form of autophagy that degrades specific substrates, such as misfolded proteins, protein aggregates, mitochondria, and invading bacteria. The process involves the interaction between autophagic adapters and the autophagosomal marker protein LC3, mediated by a LIR (LC3-interacting region) motif. This interaction, along with the ability to polymerize or aggregate and specific substrate recognition, is essential for efficient selective autophagy. The article discusses the degradation of various cellular components, including misfolded proteins, p62 bodies, aggresomes, mitochondria, and bacteria, and highlights the emerging role of selective autophagy in regulating cell signaling, oxidative stress responses, tumorigenesis, and innate immunity. The importance of p62 and NBR1 as cargo receptors for ubiquitinated substrates is emphasized, along with their involvement in bone remodeling and T-cell activation. The LIR-ATG8 (LC3/GABARAP) interaction is described in detail, including the structural basis and functional significance. The article also explores the hypothesis that p62 and NBR1 act as adapters for the selective autophagy of ubiquitinated substrates, and discusses the formation and degradation of p62 bodies, aggresomes, and other specialized structures. The role of p62 in the constitutive and stress-induced autophagy of misfolded proteins is highlighted, along with the consequences of inefficient autophagic degradation leading to the accumulation of ubiquitinated aggregates. The selective autophagy of aggregated protein substrates, such as aggresomes, and the selective removal of damaged mitochondria (mitophagy) are also covered, emphasizing the importance of specific adapters and signaling pathways in these processes.