Abstract
Brain aging is characterized by a time-dependent decline of tissue integrity and function, and it is a major risk for neurodegenerative diseases and brain cancer. Chaperone-mediated autophagy (CMA) is a selective form of autophagy specialized in protein degradation, which is based on the individual translocation of a cargo protein through the lysosomal membrane. Regulation of processes such as proteostasis, cellular energetics, or immune system activity has been associated with CMA, indicating its pivotal role in tissue homeostasis. Since first studies associating Parkinson’s disease (PD) to CMA dysfunction, increasing evidence points out that CMA is altered in both physiological and pathological brain aging. In this review article, we summarize the current knowledge regarding the impact of CMA during aging in brain physiopathology, highlighting the role of CMA in neurodegenerative diseases and glioblastoma, the most common and aggressive brain tumor in adults.
Highlights
TO AUTOPHAGYThe term ‘‘autophagy’’ comes from the Ancient Greek meaning ‘‘self-eating,’’ which refers to the catabolic processes that use the cell to recycle its own constituents within the lysosome (Yang and Klionsky, 2010; Boya et al, 2013)
We summarize the current knowledge regarding the impact of chaperone-mediated autophagy’’ (CMA) during aging in brain physiopathology, highlighting the role of CMA in neurodegenerative diseases and glioblastoma, the most common and aggressive brain tumor in adults
Selective forms of macroautophagy and microautophagy have been described (Klionsky et al, 2016), with a special interest in ‘‘chaperone-assisted selective autophagy’’ (CASA), which participates in the selective trapping of ubiquitin-positive protein aggregates via autophagosomes (Arndt et al, 2010) and ‘‘endosomal-microautophagy,’’ in which cytosolic proteins enter endosomal compartments inside vesicles generated at the surface of the late endosomes (Sahu et al, 2011)
Summary
The term ‘‘autophagy’’ comes from the Ancient Greek meaning ‘‘self-eating,’’ which refers to the catabolic processes that use the cell to recycle its own constituents within the lysosome (Yang and Klionsky, 2010; Boya et al, 2013). Further studies demonstrated the existence of another type of autophagy named ‘‘microautophagy,’’ which involves the uptake of soluble or membrane-bound material directly into the lysosome by invagination (De Duve and Wattiaux, 1966; Marzella et al, 1981). It was not until Dice et al (1986) described a proteinselective form of autophagy, identifying a pentapeptide region on ribonuclease A required for its enhanced degradation during serum deprivation. Selective forms of macroautophagy and microautophagy have been described (Klionsky et al, 2016), with a special interest in ‘‘chaperone-assisted selective autophagy’’ (CASA), which participates in the selective trapping of ubiquitin-positive protein aggregates via autophagosomes (Arndt et al, 2010) and ‘‘endosomal-microautophagy,’’ in which cytosolic proteins enter endosomal compartments inside vesicles generated at the surface of the late endosomes (Sahu et al, 2011)
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