Crystal Structure of Oxidative Stress Sensor Keap1 in Complex with Selective Autophagy Substrate p62
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- KUROKAWA Hirofumi
- Department of Medical Biochemistry, Tohoku University Graduate School of Medicine
Bibliographic Information
- Other Title
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- 酸化ストレスセンサーKeap1と選択的オートファジー基質p62複合体の結晶構造解析
- サンカ ストレスセンサー Keap1 ト センタクテキ オートファジーキシツ p62 フクゴウタイ ノ ケッショウ コウゾウ カイセキ
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Abstract
Keap1, an adaptor protein of cullin-RING ubiquitin ligase complex, represses cytoprotective transcription factor Nrf2 in an oxidative stress-dependent manner. The accumulation of selective autophagy substrate p62 also activates Nrf2 target genes, but the detailed mechanism has not been elucidated. Crystal structure of Keap1-p62 complex revealed the structural basis for the Nrf2 activation in which Keap1 is inactivated by p62. The accumulation of p62 is observed in hepatocellular carcinoma. The activation of Nrf2 target genes, including detoxifying enzymes and efflux transporters, by p62 may protect the cancer cells from anti-cancer drugs.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 52 (5), 250-254, 2010
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390001204086372608
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- NII Article ID
- 10027673083
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- NII Book ID
- AN00188364
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- COI
- 1:CAS:528:DC%2BC3MXjtFWjtg%3D%3D
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 10882227
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed