Alzheimer's disease (Alzheimer's disease, commonly referred to as AD), commonly known as Alzheimer's disease, is a degenerative disease of the central nervous system that causes cognitive impairment and memory impairment in patients, leading to deteriorating life skills and death. The late President Ronald Reagan of the United States, the former Prime Minister Margaret Thatcher of the United Kingdom, and other celebrities were plagued by the disease.
The main pathological features of AD include a large number of senile plaques (SP) formed by the deposition of β-amyloid (Aβ) in the brain and neurofibrillary tangles formed by the accumulation of hyperphosphorylated tau protein in neurons. Neofolibrary tangle, neuronal dystrophy, massive loss of neurons, synapse damage and loss. Abnormal phosphorylation of Tau protein is associated with the aggregation of Tau protein and the progression of AD. More and more evidence shows that the abnormal aggregation of Tau protein has a certain relationship with the post-translational modification of Tau protein, such as glycosylation, acetylation, ubiquitination/SUMO, and peptide proline isomerization.
Post-translational modifications of proteins include phosphorylation, acetylation, methylation, ubiquitination, and SUMOylation, which can be regulated by modulating substrate protein activity, subcellular localization, stability, or interactions with other proteins. The role of protein function. Many neurodegenerative disease-related proteins such as huntingtin, ataxin-1, α-synuclein, DJ-1, and tau, etc., have an effect on protein function and disease progression due to SUMOylation modification. Therefore, there is a great relationship between the post-translational modification of proteins and neurodegenerative diseases.
The related protein tau of Alzheimer's disease (AD) can be modified by SUMO1, and the degree of SUMO2/3 modification is weaker than SUMO1, and the SUMO site of tau K340 is in its microtubule-binding domain. Tau can not only be modified by SUMO but also ubiquitinated, and there is competition between the two to regulate the stability of tau. As more SUMO substrates are discovered, as well as more in-depth studies of SUMOylation mechanisms and functions, we will better understand the role of SUMOylation in neurodegenerative diseases.
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