| First Author | Hong Y | Year | 2012 |
| Journal | J Neurosci | Volume | 32 |
| Issue | 48 | Pages | 17262-72 |
| PubMed ID | 23197718 | Mgi Jnum | J:193052 |
| Mgi Id | MGI:5467465 | Doi | 10.1523/JNEUROSCI.3300-12.2012 |
| Citation | Hong Y, et al. (2012) SRPK2 phosphorylates tau and mediates the cognitive defects in Alzheimer's disease. J Neurosci 32(48):17262-72 |
| abstractText | 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's disease (AD) brain. Therefore, our study suggests SRPK2 may contribute to the formation of hyperphosphorylated tau and the pathogenesis of AD. |
