期刊
JOURNAL OF CELL SCIENCE
卷 135, 期 4, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.259449
关键词
mRNA export; SUMO; DDX19; Nup358; Gle1
类别
资金
- National Centre for Cell Science (NCCS)
- Department of Biotechnology, Government of India [BT/PR27451/BRB/10/1655/2018]
- Council of Scientific and Industrial Research (CSIR)
- Department of Biotechnology (DBT), Government of India
Nuclear export of mRNAs is a crucial step in eukaryotic gene expression. This study reveals that DDX19 gets covalently attached with SUMO at lysine 26, which enhances its interaction with Gle1 and fine-tunes its function in mRNA export.
Nuclear export of mRNAs is a critical regulatory step in eukaryotic gene expression. The mRNA transcript undergoes extensive processing, and is loaded with a set of RNA-binding proteins (RBPs) to form export-competent messenger ribonucleoprotein particles (mRNPs) in the nucleus. During the transit of mRNPs through the nuclear pore complex (NPC), the DEAD-box ATPase - DDX19 (herein referring to DDX19A and DDX19B) - remodels mRNPs at the cytoplasmic side of the NPC, by removing a subset of RNA-binding proteins to terminate mRNP export. This requires the RNA-dependent ATPase activity of DDX19 and its dynamic interactions with Gle1 and Nup214. However, the regulatory mechanisms underlying these interactions are unclear. We find that DDX19 gets covalently attached with a small ubiquitin-like modifier (SUMO) at lysine 26, which enhances its interaction with Gle1. Furthermore, a SUMOylation-defective mutant of human DDX19B, K26R, failed to provide a complete rescue of the mRNA export defect caused by DDX19 depletion. Collectively, our results suggest that SUMOylation fine-tunes the function of DDX19 in mRNA export by regulating its interaction with Gle1. This study identifies SUMOylation of DDX19 as a modulatory mechanism during the mRNA export process. This article has an associated First Person interview with the first author of the paper.
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