Shin, Seulgi Lim, Sungsu Jeong, Hyeanjeong Kwan, Li Ting Kim, Yun Kyung 2024-01-19T21:34:09Z 2024-01-19T21:34:09Z 2021-09-04 2018-10 1661-6596 https://pubs.kist.re.kr/handle/201004/120858 Tau is a neuron-specific microtubule-binding protein that stabilizes microtubules. It is generally thought that highly phosphorylated tau dissociates from microtubules and becomes insoluble aggregates, leading to neuronal degeneration. Due to the implication of tau aggregation in neurodegenerative disorders, including Alzheimer’s disease, great efforts have been made to identify the tau aggregation process. However, tau interaction with tubulin during the aggregation process remains largely unknown. To scrutinize the tau-tubulin interaction, we generated a cell model that enables visualization of the tau-tubulin interaction in a living cell using the Bifluorescence Complementation (BiFC) Technique. Upon diverse chemical stimulation that induced tau pathology, tau-tubulin BiFC cells showed significantly increased levels of BiFC fluorescence, indicating that tau aggregates together with tubulin. Our results suggest that tubulin should be considered as a key component in the tau aggregation process. English Multidisciplinary Digital Publishing Institute (MDPI) Visualization of Tau-Tubulin Interaction in a Living Cell Using Bifluorescence Complementation Technique Article 10.3390/ijms19102978 1 International Journal of Molecular Sciences, v.19, no.10 International Journal of Molecular Sciences 19 10 N scie scopus 000448951000133 2-s2.0-85054094910 Biochemistry & Molecular Biology Chemistry, Multidisciplinary Biochemistry & Molecular Biology Chemistry Article ALZHEIMERS-DISEASE BETA-TUBULIN BINDING-SITE MICROTUBULE DYNAMICS TAXOL BINDING AGGREGATION VINBLASTINE HETERODIMERS TAUOPATHIES NOCODAZOLE tau aggregation microtubule tubulin Bifluorescence Complementation neurodegeneration