Structural and mechanistic insights into the arginine/lysine-rich peptide motifs that interact with P97NCP
文献类型：期刊论文
| 作者 | Liu, S; Fu, QS; Zhao, J; Hu, HY |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| 出版日期 | 2013 |
| 卷号 | 1834期号:12页码:2672-2678 |
| 关键词 | P97/VCP VCP-binding motif VCP-interacting motif Arginine/lysine-rich Structure Interaction |
| 通讯作者 | Hu, HY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai 200031, Peoples R China.,hyhu@sibcb.ac.cn |
| 英文摘要 | P97 protein, also referred to as valosin-containing protein (VCP), is an AAA-ATPase (ATPase associated with a variety of cellular activities) that mediates vital cellular activities with the cooperation of many cofactors. A group of cofactors interact with the N-terminal domain of P97 (P97N) through their Arg/Lys-rich peptide motifs. We investigated the interactions between P97 and these motifs, including VCP-binding motif (VBM) and VCP-interacting motif (VIM). The solution structures of the VBM motif from HRD1 and the VIM motif from SVIP are both comprised mainly of a single alpha-helix. The VIM motifs generally have stronger P97N-binding affinities than the VBMs, and SVIP (VIM) can compete with HRD1-VBM for the interaction, providing a possibility that VIM-containing proteins (such as SVIP) act as competitors against VBM-containing proteins (such as HRD1) for interacting with P97. Based on biochemical features of the VBM motifs, we also identified NUB1L (NEDD8 ultimate buster-1 long) as a novel VBM-containing protein, which is involved in proteasomal degradation of NEDD8 through the P97 pathway. (C) 2013 Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | RETICULUM-ASSOCIATED DEGRADATION ; INCLUSION-BODY MYOPATHY ; ENDOPLASMIC-RETICULUM ; AAA ATPASE ; PROTEIN-DEGRADATION ; FRONTOTEMPORAL DEMENTIA ; UBIQUITIN LIGASE ; BINDING ; CDC48/P97 ; SYSTEM |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000329418300025 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/447]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Liu, S,Fu, QS,Zhao, J,et al. Structural and mechanistic insights into the arginine/lysine-rich peptide motifs that interact with P97NCP[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2013,1834(12):2672-2678. |
| APA | Liu, S,Fu, QS,Zhao, J,&Hu, HY.(2013).Structural and mechanistic insights into the arginine/lysine-rich peptide motifs that interact with P97NCP.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1834(12),2672-2678. |
| MLA | Liu, S,et al."Structural and mechanistic insights into the arginine/lysine-rich peptide motifs that interact with P97NCP".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1834.12(2013):2672-2678. |
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