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【期刊论文】The ubiquitin ligase Hrd1 promotes degradation of the Z variant
沈玉先, Haiping Wang, Qi Li, Yujun Shen
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-1年11月30日
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【期刊论文】Induction profile of MANF/ARMET by cerebral
沈玉先, Yong-Qiang Yu, Lian-Cheng Liu, Fa-Cai Wang, Yan Liang, Da-Qin Cha
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-1年11月30日
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沈玉先, Yong-Qiu Zheng, Wei Wei, Yu-Xian Shen, Min Dai, Li-Hua Liu
Copyright ,-0001,():
-1年11月30日
To investigate the curative effects of oral and nasal administration of chicken type II collagen (CII) on adjuvant arthritis (AA) in rats with meloxicam-induced intestinal lesions.
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沈玉先, Hua Wang, Wei Wei, Yu-Xian Shen, Chen Dong, Ling-Ling Zhang, Ni-Ping Wang, Li Yue, Shu-Yun Xu
Copyright ,-0001,():
-1年11月30日
To investigate the effects and mechanisms of melatonin on immunological liver injury in mice.
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沈玉先, Xiaoyan Zhong‡, Yuxian Shen‡, Petek Ballar‡, Andria Apostolou‡, Reuven Agami§, and Shengyun Fang‡¶
Vol. 279, No. 44, Issue of October 29, pp. 45676-45684, 2004,-0001,():
-1年11月30日
Endoplasmic reticulum-associated degradation (ERAD)is a protein quality control mechanism that eliminates unwanted proteins from the endoplasmic reticulum (ER) through a ubiquitin-dependent proteasomal degradation pathway. gp78 is a previously described ER membrane-anchored ubiquitin ligase (E3) involved in ubiquitination of ER proteins. AAA ATPase (ATPase associated with various cellular activities) p97/valosincontaining protein (VCP) subsequently dislodges the ubiquitinated proteins from the ER and chaperones them to the cytosol, where they undergo proteasomal degradation. We now report that gp78 physically interacts with p97/VCP and enhances p97/VCP-polyubiquitin association. The enhanced association correlates with decreases in ER stress-induced accumulation of olyubiquitinated proteins. This effect is abolished when the p97/VCP-interacting domain of gp78 is removed. Further, using ERAD substrate CD3, gp78 consistently enhances p97/VCP-CD3 binding and facilitates CD3 degradation. Moreover, inhibition of endogenous gp78 expression by RNA interference markedly increases the levels of total polyubiquitinated proteins, including CD3, and abrogates VCP-CD3 interactions. The gp78 mutant with deletion of its p97/VCP-interacting domain fails to increase CD3 degradation and leads to accumulation of polyubiquitinated CD3, suggesting a failure in delivering ubiquitinated CD3 for degradation. These data suggest that gp78-p97/VCP interaction may represent one way of coupling ubiquitination with retrotranslocation and degradation of ERAD substrates.
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