Abstract
Protein degradation is important for proper cellular physiology as it removes malfunctioning proteins or can provide a source for energy. Proteasomes and lysosomes, through the regulatory particles or adaptor proteins, respectively, recognize proteins destined for degradation. These systems have developed mechanisms to allow adaptation to the everchanging environment of the cell. While the complex recognition of proteins to be degraded is somewhat understood, the mechanisms that help switch the proteasomal regulatory particles or lysosomal adaptor proteins to adjust to the changing landscape of degrons, during infections or inflammation, still need extensive exploration. Therefore, this review is focused on describing the protein degradation systems and the possible sensors that may trigger the rapid adaptation of the protein degradation machinery.
Highlights
Protein homeostasis or ”proteostasis”, the balance of the synthesis and degradation of proteins, is closely associated with cellular compartments, including the Golgi apparatus, the endoplasmic reticulum (ER), and the lysosome [1]
Should the degradation of proteins be overwhelmed despite both degradation pathways being activated, unwanted proteins are sequestered into aggresomes to prevent toxicity to the cell
While the constitutive proteasome is composed of the 20S core protease (CP) and a single or double 19S cap to form the 26S and 30S proteasomes, respectively, when cells are exposed to inflammatory stimuli, such as TNF-α or IFN-γ, immunoproteasomes are assembled (Figure 2)
Summary
Protein homeostasis or ”proteostasis”, the balance of the synthesis and degradation of proteins, is closely associated with cellular compartments, including the Golgi apparatus, the endoplasmic reticulum (ER), and the lysosome [1]. The ubiquitin-proteasome and the autophagy-lysosome systems ensure selective degradation of proteins. In muscle cells, for example, autophagy can account for 40% of degradation of long-lived proteins [2]. The crosstalk between these two proteolytic pathways increases the capacity to process protein degradation and participates in the recycling of the compounds [3]. This review will focus on the mechanisms that provide the plasticity of these degradation systems to adapt to physiological changes, including viral and bacterial infections or exposure to environmental insults that increase reactive oxygen species (ROS)
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