Cytoplasmic poly(A)-binding protein 1 (PABPC1) interacts with the RNA-binding protein hnRNPLL and thereby regulates immunoglobulin secretion in plasma cells
文献类型：期刊论文
| 作者 | Peng, Yuanzheng1,2,3; Yuan, Juanjuan1,2,3; Zhang, Zhenchao1,3; Chang, Xing1,2,3; , |
| 刊名 | JOURNAL OF BIOLOGICAL CHEMISTRY
 |
| 出版日期 | 2017 |
| 卷号 | 292期号:29页码:12285-12295 |
| 关键词 | Genetic engineering Site-specific recombinase (SSR) Nigri-nox Fate mapping Cardiac valve development Genetic engineering Site-specific recombinase (SSR) Nigri-nox Fate mapping Cardiac valve development |
| ISSN号 | 0021-9258 |
| DOI | 10.1074/jbc.M117.794834 |
| 文献子类 | Article |
| 英文摘要 | Increasing evidence indicates that alternative processing of mRNA, including alternative splicing, 3 ' alternative polyadenylation, and regulation of mRNA stability/translation, represents a major mechanism contributing to protein diversification. For example, in alternative polyadenylation, the 3 ' end of the immunoglobulin heavy chain mRNA is processed during B cell differentiation, and this processing involves RNA-binding proteins. hnRNPLL (heterogeneous nuclear ribonucleoprotein L-like protein) is an RNA-binding protein expressed in terminally differentiated lymphocytes, such as memory T cells and plasma cells. hnRNPLL regulates various processes of RNA metabolism, including alternative pre-mRNA splicing and RNA stability. In plasma cells, hnRNPLL also regulates the transition from the membrane isoform of the immunoglobulin heavy-chain (mIgH) to the secreted isoform (sIgH), but the precise mechanism remains to be identified. In this study, we report that hnRNPLL specifically associates with cytoplasmic PABPC1 (poly(A)-binding protein 1) in both T cells and plasma cells. We found that although PABPC1 is not required for the alternative splicing of CD45, a primary target of hnRNPLL in lymphocytes, PABPC1 does promote the binding of hnRNPLL to the immunoglobulin mRNA and regulates switching from mIgH to sIgH in plasma cells. Given the recently identified role of PABPC1 in mRNA alternative polyadenylation, our findings suggest that PABPC1 recruits hnRNPLL to the 3 ' -end of RNA and regulates the transition from membrane Ig to secreted Ig through mRNA alternative polyadenylation. In conclusion, our study has revealed a mechanism that regulates immunoglobulin secretion in B cells via cooperation between a plasma cell-specific RBP (hnRNPLL) and a universally expressed RBP (PABPC1). |
| 学科主题 | Biochemistry & Molecular Biology |
| WOS关键词 | PRE-MESSENGER-RNA ; B-CELL ; ALTERNATIVE CLEAVAGE ; ELONGATION-FACTOR ; DIFFERENTIATION ; POLYADENYLATION ; RIBONUCLEOPROTEIN ; TRANSLATION ; TRANSCRIPTION ; REPRESSION |
| 语种 | 英语 |
| WOS记录号 | WOS:000406053300024 |
| 出版者 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.144/handle/331004/936]  |
| 专题 | 中国科学院上海生命科学研究院营养科学研究所 |
| 作者单位 | 1.Univ Chinese Acad Sci, Chinese Acad Sci, Sch Med, Shanghai Jiao Tong Univ, Shanghai 200031, Peoples R China; 2.Shanghai Jiao Tong Univ, Sch Med, Collaborat Innovat Ctr Syst Biomed, Shanghai 200031, Peoples R China, 3.Shanghai Inst Biol Sci, Inst Hlth Sci, Key Lab Stem Cell Biol, Shanghai 200031, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Peng, Yuanzheng,Yuan, Juanjuan,Zhang, Zhenchao,et al. Cytoplasmic poly(A)-binding protein 1 (PABPC1) interacts with the RNA-binding protein hnRNPLL and thereby regulates immunoglobulin secretion in plasma cells[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2017,292(29):12285-12295. |
| APA | Peng, Yuanzheng,Yuan, Juanjuan,Zhang, Zhenchao,Chang, Xing,&,.(2017).Cytoplasmic poly(A)-binding protein 1 (PABPC1) interacts with the RNA-binding protein hnRNPLL and thereby regulates immunoglobulin secretion in plasma cells.JOURNAL OF BIOLOGICAL CHEMISTRY,292(29),12285-12295. |
| MLA | Peng, Yuanzheng,et al."Cytoplasmic poly(A)-binding protein 1 (PABPC1) interacts with the RNA-binding protein hnRNPLL and thereby regulates immunoglobulin secretion in plasma cells".JOURNAL OF BIOLOGICAL CHEMISTRY 292.29(2017):12285-12295. |
入库方式： OAI收割
来源：上海营养与健康研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。