@article {Hong17262, author = {Yi Hong and Chi Bun Chan and Il-Sun Kwon and Xuekun Li and Mingke Song and Hyun-Pil Lee and Xia Liu and Pradoldej Sompol and Peng Jin and Hyoung-gon Lee and Shan Ping Yu and Keqiang Ye}, title = {SRPK2 Phosphorylates Tau and Mediates the Cognitive Defects in Alzheimer{\textquoteright}s Disease}, volume = {32}, number = {48}, pages = {17262--17272}, year = {2012}, doi = {10.1523/JNEUROSCI.3300-12.2012}, publisher = {Society for Neuroscience}, abstract = {Serine-arginine protein kinases 2 (SRPK2) is a cell cycle-regulated kinase that phosphorylates serine/arginine domain-containing proteins and mediates pre-mRNA splicing with unclear function in neurons. Here, we show that SRPK2 phosphorylates tau on S214, suppresses tau-dependent microtubule polymerization, and inhibits axonal elongation in neurons. Depletion of SRPK2 in dentate gyrus inhibits tau phosphorylation in APP/PS1 mouse and alleviates the impaired cognitive behaviors. The defective LTP in APP/PS1 mice is also improved after SRPK2 depletion. Moreover, active SRPK2 is increased in the cortex of APP/PS1 mice and the pathological structures of human Alzheimer{\textquoteright}s disease (AD) brain. Therefore, our study suggests SRPK2 may contribute to the formation of hyperphosphorylated tau and the pathogenesis of AD.}, issn = {0270-6474}, URL = {https://www.jneurosci.org/content/32/48/17262}, eprint = {https://www.jneurosci.org/content/32/48/17262.full.pdf}, journal = {Journal of Neuroscience} }