The proline-rich domain promotes Tau liquid–liquid phase separation in cells
نویسندگان
چکیده
منابع مشابه
Tau phosphorylation regulates the interaction between BIN1’s SH3 domain and Tau’s proline-rich domain
INTRODUCTION The application of high-throughput genomic approaches has revealed 24 novel risk loci for Alzheimer's disease (AD). We recently reported that the bridging integrator 1 (BIN1) risk gene is linked to Tau pathology. RESULTS We used glutathione S-transferase pull-down assays and nuclear magnetic resonance (NMR) experiments to demonstrate that BIN1 and Tau proteins interact directly a...
متن کاملThe unique proline-rich domain of parotid proline-rich proteins functions in secretory sorting.
When expressed in pituitary AtT-20 cells, parotid proline-rich proteins enter the regulated pathway. Because the short N-terminal domain of a basic proline-rich protein is necessary for efficient export from the ER, it has not been possible to evaluate the role of this polypeptide segment as a sorting signal for regulated secretion. We now show that addition of the six-amino acid propeptide of ...
متن کاملThe proline-rich domain and the microtubule binding domain of protein tau acting as RNA binding domains.
Neuronal tau, through its proline-rich domain and the microtubule binding domain, binds to RNA non-sequence-specifically via electrostatic interaction. This binding inhibits the activity of tau. Tau and RNA were also found to co-localize in SH-SY5Y cells suggesting that RNA has opportunities to interact with tau in cells.
متن کاملHistidine-proline-rich glycoprotein has potent antiangiogenic activity mediated through the histidine-proline-rich domain.
Histidine-proline-rich glycoprotein (HPRG) is an abundant multidomain plasma protein evolutionarily related to high-molecular-weight kininogen. The cleaved form of high-molecular-weight kininogen has recently been demonstrated to exhibit antiangiogenic activities in vitro (J. C. Zhang et al., FASEB J., 14: 2589-2600, 2000), mediated primarily through domain 5. HPRG contains a histidine-proline-...
متن کاملTau protein liquid–liquid phase separation can initiate tau aggregation
The transition between soluble intrinsically disordered tau protein and aggregated tau in neurofibrillary tangles in Alzheimer's disease is unknown. Here, we propose that soluble tau species can undergo liquid-liquid phase separation (LLPS) under cellular conditions and that phase-separated tau droplets can serve as an intermediate toward tau aggregate formation. We demonstrate that phosphoryla...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2020
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.202006054