Tripartite Management of Unfolded Proteins in the Endoplasmic Reticulum
書誌事項
- 公開日
- 2000-05
- 権利情報
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- https://www.elsevier.com/tdm/userlicense/1.0/
- https://www.elsevier.com/open-access/userlicense/1.0/
- DOI
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- 10.1016/s0092-8674(00)80855-7
- 公開者
- Elsevier BV
この論文をさがす
説明
The cellular responses to the accumulation of unfolded proteins in the ER are much more extensive than previously recognized. Three disparate defense systems respond to signals emanating from the ER. These systems work in a coordinated fashion to improve the efficiency of folding, processing, and export of secretory proteins, to remove the fraction of polypeptides that fail to fold, and to reduce the flow of proteins into the ER compartment. Interestingly, two groups recently reported that the UPR is weakened in cells carrying a mutation or deletion of presenilin-1 involved in Alzheimer's disease (10xKatayama, T, Imaizumi, K, Sato, N, Miyoshi, K, Kudo, T, Hitomi, J, Morihara, T, Yoneda, T, Gomi, F, Mori, Y et al. Nat. Cell Biol. 1999; 1: 479–485Crossref | PubMedSee all References, 13xNiwa, M, Sidrauski, C, Kaufman, R.J, and Walter, P. Cell. 1999; 99: 691–702Abstract | Full Text | Full Text PDF | PubMedSee all References). Consistent with this finding, compared to age-matched controls, the brains of sporadic and familial Alzheimer's disease patients contained significantly less BiP/GRP78 and GRP94 (Katayama et al. 1999xKatayama, T, Imaizumi, K, Sato, N, Miyoshi, K, Kudo, T, Hitomi, J, Morihara, T, Yoneda, T, Gomi, F, Mori, Y et al. Nat. Cell Biol. 1999; 1: 479–485Crossref | PubMedSee all ReferencesKatayama et al. 1999). Under normal circumstances, these chaperones may play a central role in suppressing the formation of amyloidogenic peptides in the ER (see review by Gething 2000xGething, M.-J. Nat. Cell Biol. 2000; 2: E21–E23Crossref | PubMed | Scopus (9)See all ReferencesGething 2000). Thus, further understanding of the three cellular responses will provide new insights into not only fundamental principles in cell biology but also the pathogenesis of diseases that result from problems in protein folding in the ER.*E-mail: kazumori@ip.media.kyoto-u.ac.jp
収録刊行物
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- Cell
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Cell 101 (5), 451-454, 2000-05
Elsevier BV
