No full admission for tau to the exclusive prion club yet

Polanco, Juan Carlos and Götz, Jürgen (2015) No full admission for tau to the exclusive prion club yet. EMBO Journal, 34 24: 2990-2992. doi:10.15252/embj.201593311


Author Polanco, Juan Carlos
Götz, Jürgen
Title No full admission for tau to the exclusive prion club yet
Journal name EMBO Journal   Check publisher's open access policy
ISSN 1460-2075
0261-4189
Publication date 2015-11-09
Year available 2015
Sub-type Article (original research)
DOI 10.15252/embj.201593311
Open Access Status Not yet assessed
Volume 34
Issue 24
Start page 2990
End page 2992
Total pages 3
Place of publication Oxford, United Kingdom
Publisher Wiley-Blackwell Publishing
Collection year 2016
Language eng
Abstract Aggregation of the microtubule‐associated protein tau is a key feature of Alzheimer's disease and other so‐called tauopathies, yet what causes this protein to aggregate and what renders it toxic is only slowly being revealed. Because tau spreads in a stereotypical pattern through the diseased brain, it has been proposed that it possesses prion‐like properties, with aggregation‐prone tau facilitating the conversion of “naïve” tau into “toxic” forms. The current study by Wegmann et al (2015) addresses whether tau fulfils classical “prion criteria” by assessing its spreading and toxicity in the absence of endogenous tau. Using different transgenic and viral paradigms, the authors demonstrate that, although tau still propagates in this scenario, there is a decrease in its misfolding and neurotoxicity. They therefore conclude that tau is not a genuine prion, at least when the current definition of these infectious proteins is applied.
Q-Index Code CX
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
Queensland Brain Institute Publications
 
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Created: Wed, 09 Dec 2015, 15:03:13 EST by Susan Day on behalf of Queensland Brain Institute