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ELYS regulates the localization of LBR by modulating its phosphorylation state

阿平添加于 2016-11-18 17:58 | 1204 次阅读 | 0 个评论

作者
Mimura Y, Takagi M, Clever M, Imamoto N
摘要
Lamin B receptor (LBR), an inner nuclear membrane (INM) protein, contributes to the functional integrity of the nucleus by tethering heterochromatin to the nuclear envelope. We have previously reported that the depletion of embryonic large molecule derived from yolk sac (ELYS; also known as AHCTF1), a component of the nuclear pore complex, from cells perturbs the localization of LBR to the INM, but little is known about the underlying molecular mechanism. In this study, we found that the depletion of ELYS promoted LBR phosphorylation at the residues known to be phosphorylated by cyclin-dependent kinase (CDK) and serine/arginine protein kinases 1 and 2 (SRPK1 and SRPK2, respectively). These phosphorylation events were most likely to be counter-balanced by protein phosphatase 1 (PP1), and the depletion of PP1 from cells consistently caused the mislocalization of LBR. These observations point to a new mechanism regulating the localization of LBR, which is governed by an ELYS-mediated phosphorylation network. This phosphorylation-dependent coordination between INM proteins and the nuclear pore complex might be important for the integrity of the nucleus.
详细资料
- 关键词: Inner nuclear membrane protein; Nuclear envelope; Nuclear pore complex; Nucleoporin; Phosphorylation
- 文献种类: Journal Article
- 期刊名称: Journal of Cell Science
- 期刊缩写: J Cell Sci
- 期卷页: 2016年第129卷第22期 4200-4212页
- 地址: Cellular Dynamics Laboratory, Riken, Saitama 351-0198, Japan nimamoto@riken.jp
- ISBN: 0021-9533
学科领域生物医药 » 生物学
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