共查询到20条相似文献,搜索用时 31 毫秒
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ER stress signaling by regulated proteolysis of ATF6 总被引:3,自引:0,他引:3
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Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response 总被引:26,自引:0,他引:26
Wang Y Shen J Arenzana N Tirasophon W Kaufman RJ Prywes R 《The Journal of biological chemistry》2000,275(35):27013-27020
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Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response 总被引:4,自引:0,他引:4
Hong M Luo S Baumeister P Huang JM Gogia RK Li M Lee AS 《The Journal of biological chemistry》2004,279(12):11354-11363
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ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs 总被引:20,自引:0,他引:20
Ye J Rawson RB Komuro R Chen X Davé UP Prywes R Brown MS Goldstein JL 《Molecular cell》2000,6(6):1355-1364
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Satoshi Horimoto Satoshi Ninagawa Tetsuya Okada Hibiki Koba Takehiro Sugimoto Yukiko Kamiya Koichi Kato Shunichi Takeda Kazutoshi Mori 《The Journal of biological chemistry》2013,288(44):31517-31527
Proteins misfolded in the endoplasmic reticulum (ER) are cleared by the ubiquitin-dependent proteasome system in the cytosol, a series of events collectively termed ER-associated degradation (ERAD). It was previously shown that SEL1L, a partner protein of the E3 ubiquitin ligase HRD1, is required for degradation of misfolded luminal proteins (ERAD-Ls substrates) but not misfolded transmembrane proteins (ERAD-Lm substrates) in both mammalian and chicken DT40 cells. Here, we analyzed ATF6, a type II transmembrane glycoprotein that serves as a sensor/transducer of the unfolded protein response, as a potential ERAD-Lm substrate in DT40 cells. Unexpectedly, degradation of endogenous ATF6 and exogenously expressed chicken and human ATF6 by the proteasome required SEL1L. Deletion analysis revealed that the luminal region of ATF6 is a determinant for SEL1L-dependent degradation. Chimeric analysis showed that the luminal region of ATF6 confers SEL1L dependence on type I transmembrane protein as well. In contrast, degradation of other known type I ERAD-Lm substrates (BACE457, T-cell receptor-α, CD3-δ, and CD147) did not require SEL1L. Thus, ATF6 represents a novel type of ERAD-Lm substrate requiring SEL1L for degradation despite its transmembrane nature. In addition, endogenous ATF6 was markedly stabilized in wild-type cells treated with kifunensine, an inhibitor of α1,2-mannosidase in the ER, indicating that degradation of ATF6 requires proper mannose trimming. Our further analyses revealed that the five ERAD-Lm substrates examined are classified into three subgroups based on their dependence on mannose trimming and SEL1L. Thus, ERAD-Lm substrates are degraded through much more diversified mechanisms in higher eukaryotes than previously thought. 相似文献
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