NEDD8 Ultimate Buster-1 Long (NUB1L) Protein Promotes Transfer of NEDD8 to Proteasome for Degradation through the P97UFD1/NPL4 Complex

被引：20

作者：

Liu, Shuai ^{[1
]}

Yang, Hui ^{[1
]}

Zhao, Jian ^{[1
]}

Zhang, Yu-Hang ^{[1
]}

Song, Ai-Xin ^{[1
]}

Hu, Hong-Yu ^{[1
]}

机构：

[1] Chinese Acad Sci, State Key Lab Mol Biol, Inst Biochem & Cell Biol, Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2013年 / 288卷 / 43期

基金：

中国国家自然科学基金;

关键词：

P97 AAA ATPASE; SYNPHILIN-1-BINDING PROTEIN; CONFORMATIONAL-CHANGES; UBIQUITIN; BINDING; FAT10; DOMAINS; SYSTEM; CDC48; IDENTIFICATION;

D O I：

10.1074/jbc.M113.484816

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The NEDD8 protein and neddylation levels in cells are modulated by NUB1L or NUB1 through proteasomal degradation, but the underlying molecular mechanism is not well understood. Here, we report that NUB1L down-regulated the protein levels of NEDD8 and neddylation through specifically recognizing NEDD8 and P97/VCP. NUB1L directly interacted with NEDD8, but not with ubiquitin, on the key residue Asn-51 of NEDD8 and with P97/VCP on its positively charged VCP binding motif. In coordination with the P97-UFD1-NPL4 complex (P97(UFD1/NPL4)), NUB1L promotes transfer of NEDD8 to proteasome for degradation. This mechanism is also exemplified by the canonical neddylation of cullin 1 for SCF (SKP1-cullin1-F-box) ubiquitin E3 ligases that is exquisitely regulated by the turnover of NEDD8.

引用

页码：31339 / 31349

页数：11

共 8 条

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