Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Alzheimer's disease (AD) and frontotemporal dementias (FTDs) are popular in elderly people around the world, and both relate to the pathology of microtubule-associated protein Tau. When Tau protein is hyperphosphorylated, it detaches from the microtubule and forms the pathological aggregates. Scientists have identified a positive aggregation modifier, human SERF1a (hSERF1a), which will accelerate the aggregation process of amyloid proteins, such as alpha-synuclein and Huntingtin. By using in vitro Thioflavin-T assay, we observe hSERF1a is able to accelerate the in vitro aggregation of human full-length Tau protein (hTau441). To investigate hSERF1a in vivo, we use fly Tau model. Drosophila genome contains an annotated gene CG17931, which shows evident homology to hSERF1a, so we predict it may preserve a similar function. We harnessed RNAi strategy to reduce the expression level of endogenous CG17931 in hTau441-expressing fly and observed the rough eye phenotype caused by hTau441 cytotoxicity was enhanced. Although the result was against our hypothesis, previous studies have suggested Tau oligomer is more toxic than neurofibrillary tangles (NFTs) in mouse models and post-mortem patient brains, which can explain our observations. While my study is ongoing, our results demonstrate the interaction between CG17931/hSERF1a and hTau441 could stand for the hypothetic mechanism of tauopathy and its future clinical implications. The poster was presented at 2016 NTHU Life Science Symposium and awarded the first pirze.



Publication Date