Title

SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination.

Journal

Proceedings of the National Academy of Sciences of the United States of America

Volume

111

Issue

None

Pages

16586-91

Date

2014-11-18

Authors

Wang JZ | Luo HB | Feng Y | Jiang J | Liu XH | Liu ZC | Shu XJ | Wang XC | Xia YY | Xiong YS | Ye K | Yin G | Yu G | Zeng K

Furthermore, the enhanced SUMO-immunoreactivity, costained with the hyperphosphorylated tau, is detected in cerebral cortex of the AD brains, and β-amyloid exposure of rat primary hippocampal neurons induces a dose-dependent SUMOylation of the hyperphosphorylated tau. Our findings suggest that tau SUMOylation reciprocally stimulates its phosphorylation and inhibits the ubiquitination-mediated tau degradation, which provides a new insight into the AD-like tau accumulation.

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