Abstract
Neuronal aging is associated with numerous diseases resulting in memory impairment and functional decline. A common hallmark of these disorders is the accumulation of intracellular and extracellular protein aggregates. The retromer complex plays a central role in sorting proteins by marking them for reuse rather than degradation. Retromer dysfunction has been shown to induce protein aggregates and neurodegeneration, suggesting that it may be important for age-related neuronal decline and disease progression. Despite this, little is known about how aging influences retromer stability and the proteins with which it interacts. Detailed insights into age-dependent changes in retromer structure and function could provide valuable information towards treating and preventing many age-related neurodegenerative disorders. Here, we visit age-related pathways which interact with retromer function that ought to be further explored to determine its role in age-related neurodegeneration.
Highlights
Neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s are among the most prevalent age-related disorders [1,2,3,4]
Clinical trials for treatments based on the clearance of these aggregates have proven disappointing [7], sparking investigations to find other means to stave off these age-related detriments
Proper protein trafficking is essential for neuronal health as well as the processing of proteins which aggregate in neuronal decline [8]
Summary
Neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s are among the most prevalent age-related disorders [1,2,3,4]. Keywords Retromer complex · Aging · Protein trafficking · Neurodegeneration · Alzheimer’s disease · Parkinson’s disease · Autophagy It is known to be important for age-related neuronal homeostasis [15], yet nothing is known about how the complex and its function are affected by age.
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