Tau N-Terminal Inserts Regulate Tau Liquid-Liquid Phase Separation and Condensates Maturation in a Neuronal Cell Model
| العنوان: | Tau N-Terminal Inserts Regulate Tau Liquid-Liquid Phase Separation and Condensates Maturation in a Neuronal Cell Model |
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| المؤلفون: | Qiong Liu, Junyi Zhao, Qiulong Tan, Qiuping Wu, Shifeng Xiao, Chengchen Wu |
| المصدر: | International Journal of Molecular Sciences, Vol 22, Iss 9728, p 9728 (2021) International Journal of Molecular Sciences Volume 22 Issue 18 |
| بيانات النشر: | MDPI AG, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | liquid–liquid phase separation, QH301-705.5, Liquid-Liquid Extraction, Tau protein, Fluorescent Antibody Technique, tau Proteins, Protein aggregation, Protein Aggregation, Pathological, Article, Catalysis, Cell Line, protein aggregation, tau isoforms, Inorganic Chemistry, Protein Aggregates, mental disorders, medicine, Humans, Protein Isoforms, Liquid liquid, Biology (General), Physical and Theoretical Chemistry, QD1-999, Molecular Biology, Spectroscopy, Neurons, biology, Chemistry, Organic Chemistry, Colocalization, General Medicine, Human brain, Computer Science Applications, Tau isoforms, medicine.anatomical_structure, Cell culture, Cytoplasm, Biophysics, biology.protein, p62 protein, Biomarkers, Protein Binding |
| الوصف: | The microtubule-associated protein tau can undergo liquid–liquid phase separation (LLPS) to form membraneless condensates in neurons, yet the underlying molecular mechanisms and functions of tau LLPS and tau droplets remain to be elucidated. The human brain contains mainly 6 tau isoforms with different numbers of microtubule-binding repeats (3R, 4R) and N-terminal inserts (0N, 1N, 2N). However, little is known about the role of N-terminal inserts. Here we observed the dynamics of three tau isoforms with different N-terminal inserts in live neuronal cell line HT22. We validated tau LLPS in cytoplasm and found that 2N-tau forms liquid-like, hollow-shell droplets. Tau condensates became smaller in 1N-tau comparing with 2N-tau, while no obvious tau accumulated dots were shown in 0N-tau. The absence of N-terminal inserts significantly affected condensate colocalization of tau and p62. The results reveal insights into the tau LLPS assembly mechanism and functional effects of N-terminal inserts in tau. |
| وصف الملف: | application/pdf |
| تدمد: | 1422-0067 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c16ef9a565ef578cc86bb16337572a10 https://doi.org/10.3390/ijms22189728 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....c16ef9a565ef578cc86bb16337572a10 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14220067 |
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