Amyloid-like oligomerization of AIMP2 contributes to α-synuclein interaction and Lewy-like inclusion
نویسندگان
چکیده
منابع مشابه
Serine 129 Phosphorylation of α-Synuclein Cross-Links with Tissue Transglutaminase to Form Lewy Body-Like Inclusion Bodies
Intraneuronal depositions of α-synuclein have been implicated in the pathogenesis of Parkinsons's disease (PD). Previous reports have identified the crosslinking between α-synuclein and tTG (tissue transglutaminase) in both PD patients and the cellular model. However, no researches have been conducted to further investigate their interaction in physiological conditions. To address this question...
متن کاملFormation of α-synuclein Lewy neurite–like aggregates in axons impedes the transport of distinct endosomes
Aggregates of α-synuclein (α-syn) accumulate in neurons in Parkinson's disease and other synucleinopathies. These inclusions predominantly localize to axons even in the early stages of the disease, but their affect on axon function has remained unknown. Previously we established a model in which the addition of preformed α-syn fibrils to primary neurons seeds formation of insoluble α-syn inclus...
متن کاملp62/SQSTM1-Dependent Autophagy of Lewy Body-Like α-Synuclein Inclusions
α-Synuclein is the main component of Lewy bodies, the intraneuronal inclusion bodies characteristic of Parkinson's disease. Although α-synuclein accumulation is caused by inhibition of proteasome and autophagy-lysosome, the degradation of α-synuclein inclusions is still unknown. Formation of Lewy body-like inclusions can be replicated in cultured cells by introducing α-synuclein fibrils generat...
متن کاملα-Synuclein Alters Toll-Like Receptor Expression
Parkinson's disease, an age-related neurodegenerative disorder, is characterized by the loss of dopamine neurons in the substantia nigra, the accumulation of α-synuclein in Lewy bodies and neurites, and neuroinflammation. While the exact etiology of sporadic Parkinson's disease remains elusive, a growing body of evidence suggests that misfolded α-synuclein promotes inflammation and oxidative st...
متن کاملBacterial Inclusion Bodies Contain Amyloid-Like Structure
Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can be composed of native globular molecules, such as the hemoglobin molecules in sickle-cell fibrils, or can be reorganized beta-sheet-rich aggre...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Science Translational Medicine
سال: 2020
ISSN: 1946-6234,1946-6242
DOI: 10.1126/scitranslmed.aax0091