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dc.contributor.authorZhang, X.zh_CN
dc.contributor.authorLi, F.zh_CN
dc.contributor.authorBulloj, A.zh_CN
dc.contributor.authorZhang, Y. W.zh_CN
dc.contributor.authorTong, G.zh_CN
dc.contributor.authorZhang, Z.zh_CN
dc.contributor.authorLiao, F. F.zh_CN
dc.contributor.authorXu, H.zh_CN
dc.contributor.author张云武zh_CN
dc.date.accessioned2013-12-12T02:25:42Z
dc.date.available2013-12-12T02:25:42Z
dc.date.issued2006zh_CN
dc.identifier.citationFASEB J,20(8):1272-4zh_CN
dc.identifier.issn1530-6860zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/66009
dc.description.abstractNeurofibrillary tangles (NFTs), consisting of abnormally hyperphosphorylated tau, are implicated in the pathogenesis of several neurodegenerative diseases including Alzheimer's disease (AD). The molecular mechanisms underlying the regulation of tau phosphorylation are largely unknown. While the PI3K/ Akt pathway has been shown to regulate multiple cellular events pertinent to AD pathogenesis, potential functions of tumor suppressor phosphatase and tensin homologue deleted on chromosome 10 (PTEN) in AD pathogenesis have not been explored. Here, we examine the effects of PTEN on tau phosphorylation, its microtubule association and formation of aggregates, and consequentially neuronal morphology. In cultured cells, overexpression of wild-type (WT) PTEN alters tau phosphorylation at several sites, increases tau-microtubule association and decreases formation of tau aggregates. In addition, the phosphatase-null PTEN increases tau aggregation and impairs tau binding to microtubule and neurite outgrowth of neurons expressing the mutant PTEN. We also found a significant loss of PTEN in AD patient brains correlated with a dramatically increased concentration of phospho-tau at Ser-214 in NFTs. Together, our results demonstrate that PTEN regulates tau phosphorylation, binding to micro-tubules and formation of aggregates and neurite outgrowth. These findings suggest a link between malfunction of PTEN and tauopathy, and imply PTEN as a therapeutic target for tauopathy.-Zhang, X., Li, F., Bulloj, A., Zhang, Y.-w., Tong, G., Zhang, Z., Liao, F.-F., Xu, H. Tumor-suppressor PTEN affects tau phosphorylation, aggregation, and binding to microtubules.zh_CN
dc.language.isoen_USzh_CN
dc.subjectAlzheimer's diseasezh_CN
dc.subjecttauopathyzh_CN
dc.subjectPIP3/Aktzh_CN
dc.titleTumor-suppressor PTEN affects tau phosphorylation, aggregation, and binding to microtubuleszh_CN
dc.typeArticlezh_CN


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