Site-specific phosphorylation of tau inhibits amyloid-β toxicity in Alzheimer’s mice
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- Arne Ittner
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Sook Wern Chua
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Josefine Bertz
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Alexander Volkerling
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Julia van der Hoven
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Amadeus Gladbach
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Magdalena Przybyla
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Mian Bi
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Annika van Hummel
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Claire H. Stevens
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Stefania Ippati
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Lisa S. Suh
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Alexander Macmillan
- Biomedical Imaging Facility, Mark Wainwright Analytical Centre, UNSW, Sydney, New South Wales 2052, Australia.
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- Greg Sutherland
- Discipline of Pathology, Sydney Medical School, University of Sydney, Sydney, New South Wales 2050, Australia.
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- Jillian J. Kril
- Discipline of Pathology, Sydney Medical School, University of Sydney, Sydney, New South Wales 2050, Australia.
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- Ana P. G. Silva
- School of Molecular Bioscience, University of Sydney, Sydney, New South Wales 2050, Australia.
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- Joel P. Mackay
- School of Molecular Bioscience, University of Sydney, Sydney, New South Wales 2050, Australia.
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- Anne Poljak
- Biomedical Mass Spectrometry Facility, Mark Wainwright Analytical Centre, UNSW, Sydney, New South Wales 2052, Australia.
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- Fabien Delerue
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
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- Yazi D. Ke
- Motor Neuron Disease Unit, School of Medical Sciences, UNSW, Sydney, New South Wales 2052, Australia.
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- Lars M. Ittner
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
書誌事項
- 公開日
- 2016-11-18
- DOI
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- 10.1126/science.aah6205
- 公開者
- American Association for the Advancement of Science (AAAS)
この論文をさがす
説明
<jats:title>Tau phosphorylation—not all bad</jats:title> <jats:p> Alzheimer's disease presents with amyloid-β (Aβ) plaques and tau tangles. The prevailing idea in the field is that Aβ induces phosphorylation of tau, which in turn mediates neuronal dysfunction. Working in Alzheimer's disease mouse models, Ittner <jats:italic toggle="yes">et al.</jats:italic> found evidence for a protective role of tau in early Alzheimer's disease. This protection involves specific tau phosphorylation at threonine 205 at the postsynapse. A protective role of phosphorylated tau in disease challenges the dogma that tau phosphorylation only mediates toxic processes. </jats:p> <jats:p> <jats:italic toggle="yes">Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6314" page="904" related-article-type="in-this-issue" vol="354" xlink:href="10.1126/science.aah6205">904</jats:related-article> </jats:p>
収録刊行物
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- Science
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Science 354 (6314), 904-908, 2016-11-18
American Association for the Advancement of Science (AAAS)
