2015年10月
Identification of key amino acids responsible for the distinct aggregation properties of microtubule-associated protein 2 and tau
JOURNAL OF NEUROCHEMISTRY
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- 巻
- 135
- 号
- 1
- 開始ページ
- 19
- 終了ページ
- 26
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1111/jnc.13228
- 出版者・発行元
- WILEY-BLACKWELL
The carboxyl-terminal sequence of tau composes the framework for its intracellular inclusions that appear in diverse neurodegenerative disorders known as tauopathies. However, microtubule-associated protein 2 (MAP2), which contains a homologous carboxyl-terminal sequence of tau, is undetectable in the mature tau inclusions. The mechanisms underlying this phenomenon have remained largely unknown. Here, we show that tau and MAP2 have different aggregation properties: tau aggregates to form filaments but MAP2 remains to be granules. Exchanging (YKPV224)-Y-221 of tau (0N3R) near the PHF6 motif for (TKKI343)-T-340 of MAP2c profoundly changed aggregation properties, suggesting that the YKPV motif is important for filament formation, whereas the TKKI motif is for granule formation. Thus, these minimal sequences may determine the different fates of tau and MAP2 in the formation of inclusions in tauopathies.
- リンク情報
- ID情報
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- DOI : 10.1111/jnc.13228
- ISSN : 0022-3042
- eISSN : 1471-4159
- Web of Science ID : WOS:000362828000003