The E3 ubiquitin ligase CHIP mediates ubiquitination and proteasomal degradation of PRMT5
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- 作者：Huan-Tian Zhanga ; b ; Ling-Fei Zengb ; c ; Qing-Yu Hed ; W. Andy Taob ; c ; Zhen-Gang Zhaa ; zhzgg@vip.163.com" class="auth_mail" title="E-mail the corresponding author ; Chang-Deng Hub ; hu1@purdue.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：PRMT5 ; protein arginine methyltransferase 5 ; EGFR ; epidermal growth factor receptor ; TNF ; tumor necrosis factor ; NF-Y ; nuclear factor Y ; PKC ; protein kinase C ; Hsp90 ; heat shock protein 90 ; UPS ; ubiquitin&ndash ; proteasome system ; CHIP ; carboxyl terminus of heat shock cognate 70-interacting protein ; TPR ; tetratricopeptide repeat ; Hsp70 ; heat shock protein 70 ; HEK293T ; human embryonic kidney 293 ; T ; CHX ; cycloheximide ; PMA ; phorbol-12-myristate-13-acetate ; GA ; geldanamycin ; 17-AAG ; 17-(Allylam
- 刊名：Biochimica et Biophysica Acta (BBA)-Molecular Cell Research
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：1863
- 期：2
- 页码：335-346
- 全文大小：1827 K
文摘
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PRMT5 undergoes polyubiquitination in LNCaP cells.
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10">The E3 ubiquitin ligase CHIP interacts with PRMT5 both in vivo and in vitro.
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15">CHIP/chaperone system mediates the ubiquitination and proteasomal degradation of PRMT5.
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CHIP mediates the inhibitory effect of 17-AAG on cell growth and down-regulation of PRMT5.