التفاصيل البيبلوغرافية
العنوان:
Differential expression, distinct localization and opposite effect on Golgi structure and cell differentiation by a novel splice variant of human PRMT5
المؤلفون:
Muhammad Sohail , David W. Litchfield , Lisheng Wang , Manli Zhang , Sam Kung , Jiuyong Xie
المصدر:
Biochemistry Publications
سنة النشر:
2015
مصطلحات موضوعية:
Gene isoform , Protein-Arginine N-Methyltransferases , Cellular differentiation , Giantin , Golgi Apparatus , Dendritic cell differentiation , Biology , Cell cycle , Gene Expression Regulation, Enzymologic , symbols.namesake , Humans , Mitosis , Molecular Biology , Protein arginine methyltransferase 5 , Alternative splicing , Golgi Matrix Proteins , Membrane Proteins , Cell Differentiation , Cell Biology , Golgi apparatus , Cell biology , Alternative Splicing , Protein Transport , HEK293 Cells , symbols , PRMT5 , Ectopic expression , Golgi structure , Dendritic cell , HeLa Cells
الوصف:
© 2015 Elsevier B.V. Alternative splicing contributes greatly to the proteomic diversity of metazoans. Protein arginine methyltransferase 5 (PRMT5) methylates arginines of Golgi components and other factors exerting diverse effects on cell growth/differentiation, but the underlying molecular basis for its subcellular distribution and diverse roles has not been fully understood. Here we show the detailed properties of an evolutionarily emerged splice variant of human PRMT5 (PRMT5S) that is distinct from the original isoform (PRMT5L). The isoforms are differentially expressed among mammalian cells and tissues. The PRMT5S is distributed all over the cell but PRMT5L mainly colocalizes with Giantin, a Golgi marker. PRMT5 knockdown led to an enlarged Giantin pattern, which was prevented by the expression of either isoform. Rescuing PRMT5S also increased the percentage of cells with an interphase Giantin pattern compacted at one end of the nucleus, consistent with its cell cycle-arresting effect, while rescuing PRMT5L increased that of the mitotic Giantin patterns of dynamically fragmented structures. Moreover, the isoforms are differentially expressed during neuronal or dendritic cell differentiation, and their ectopic expression showed an opposite effect on dendritic cell differentiation. Furthermore, besides their differential regulation of gene expression, both isoforms also similarly regulate over a thousand genes particularly those involved in apoptosis and differentiation. Taking these properties together, we propose that their differential expression and subcellular localization contribute to spatial and temporal regulation of arginine methylation and gene expression to exert different effects. The novel PRMT5S likely contributes to the observed diverse effects of PRMT5 in cells.
تدمد:
0006-3002
الوصول الحر:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e3ba244ed43d945f154f88ee8eb40edTest https://pubmed.ncbi.nlm.nih.gov/26151339Test
حقوق:
OPEN
رقم الانضمام:
edsair.doi.dedup.....3e3ba244ed43d945f154f88ee8eb40ed
قاعدة البيانات:
OpenAIRE
