Tak, HyeJin Haque, Md Mamunul Kim, Min Jung Lee, Joo Hyun Baik, Ja-Hyun Kim, YoungSoo Kim, Dong Jin Grailhe, Regis Kim, Yun Kyung 2024-01-20T11:01:16Z 2024-01-20T11:01:16Z 2022-01-10 2013-12-02 1932-6203 https://pubs.kist.re.kr/handle/201004/127341 Abnormal tau aggregation is a pathological hallmark of many neurodegenerative disorders and it is becoming apparent that soluble tau aggregates play a key role in neurodegeneration and memory impairment. Despite this pathological importance, there is currently no single method that allows monitoring soluble tau species in living cells. In this regard, we developed a cell-based sensor that visualizes tau self-assembly. By introducing bimolecular fluorescence complementation (BiFC) technique to tau, we were able to achieve spatial and temporal resolution of tau-tau interactions in a range of states, from soluble dimers to large aggregates. Under basal conditions, tau-BiFC cells exhibited little fluorescence intensity, implying that the majority of tau molecules exist as monomers. Upon chemically induced tau hyperphosphorylation, BiFC fluorescence greatly increased, indicating an increased level of tau-tau interactions. As an indicator of tau assembly, our BiFC sensor would be a useful tool for investigating tau pathology. English PUBLIC LIBRARY SCIENCE NEURITE OUTGROWTH PROTEIN-KINASE PHOSPHORYLATION MICROTUBULES AGGREGATION ACTIVATION BINDING ASSAY NEURODEGENERATION FORSKOLIN Bimolecular Fluorescence Complementation; Lighting-Up Tau-Tau Interaction in Living Cells Article 10.1371/journal.pone.0081682 1 PLOS ONE, v.8, no.12 PLOS ONE 8 12 scie scopus 000327944500087 2-s2.0-84891427788 Multidisciplinary Sciences Science & Technology - Other Topics Article MICROTUBULES AGGREGATION ACTIVATION BINDING ASSAY NEURODEGENERATION FORSKOLIN NEURITE OUTGROWTH PROTEIN-KINASE PHOSPHORYLATION tau BiFC interaction oligomerization real time