دورية أكاديمية

Nucleoporin Nup98 is an essential factor for ipo4 dependent protein import.

التفاصيل البيبلوغرافية
العنوان: Nucleoporin Nup98 is an essential factor for ipo4 dependent protein import.
المؤلفون: Guo Y; State Key Laboratory of Stress Cell Biology, School of Life Sciences, Xiamen University, Xiame, Fujian, China., Tao T; State Key Laboratory of Stress Cell Biology, School of Life Sciences, Xiamen University, Xiame, Fujian, China., Wu T; Department of Basic Medicine, School of Medicine, Cancer Research Center, Xiamen University, Xiamen, Fujian, China., Hou J; State Key Laboratory of Stress Cell Biology, School of Life Sciences, Xiamen University, Xiame, Fujian, China.; Department of Gastrointestinal Surgery, School of Medicine, Zhongshan Hospital of Xiamen University, Xiamen University, Xiamen, Fujian, China., Lin W; State Key Laboratory of Stress Cell Biology, School of Life Sciences, Xiamen University, Xiame, Fujian, China.
المصدر: Journal of cellular biochemistry [J Cell Biochem] 2024 Jul; Vol. 125 (7), pp. e30573. Date of Electronic Publication: 2024 May 23.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Wiley-Liss Country of Publication: United States NLM ID: 8205768 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-4644 (Electronic) Linking ISSN: 07302312 NLM ISO Abbreviation: J Cell Biochem Subsets: MEDLINE
أسماء مطبوعة: Publication: <2004>- : Hoboken, NJ : Wiley-Liss
Original Publication: New York : Liss, c1982-
مواضيع طبية MeSH: Active Transport, Cell Nucleus* , beta Karyopherins*/metabolism , beta Karyopherins*/genetics , Nuclear Pore Complex Proteins*/metabolism , Nuclear Pore Complex Proteins*/genetics, Humans ; Cell Nucleus/metabolism ; HeLa Cells ; Protein Binding
مستخلص: Nucleocytoplasmic transport of macromolecules is essential in eukaryotic cells. In this process, the karyopherins play a central role when they transport cargoes across the nuclear pore complex. Importin 4 belongs to the karyopherin β family. Many studies have focused on finding substrates for importin 4, but no direct mechanism studies of its precise transport function have been reported. Therefore, this paper mainly aimed to study the mechanism of nucleoporins in mediating nuclear import and export of importin 4. To address this question, we constructed shRNAs targeting Nup358, Nup153, Nup98, and Nup50. We found that depletion of Nup98 resulted in a shift in the subcellular localization of importin 4 from the cytoplasm to the nucleus. Mutational analysis demonstrated that Nup98 physically and functionally interacts with importin 4 through its N-terminal phenylalanine-glycine (FG) repeat region. Mutation of nine of these FG motifs to SG motifs significantly attenuated the binding of Nup98 to importin 4, and we further confirmed the essential role of the six FG motifs in amino acids 121-360 of Nup98 in binding with importin 4. In vitro transport assay also confirmed that VDR, the substrate of importin 4, could not be transported into the nucleus after Nup98 knockdown. Overall, our results showed that Nup98 is required for efficient importin 4-mediated transport. This is the first study to reveal the mechanism of importin 4 in transporting substrates into the nucleus.
(© 2024 Wiley Periodicals LLC.)
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فهرسة مساهمة: Keywords: Nup98; importin 4; nuclear import; nuclear pore complex
المشرفين على المادة: 0 (beta Karyopherins)
0 (Nuclear Pore Complex Proteins)
0 (Nup98 protein, human)
0 (IPO4 protein, human)
تواريخ الأحداث: Date Created: 20240523 Date Completed: 20240711 Latest Revision: 20240801
رمز التحديث: 20240801
DOI: 10.1002/jcb.30573
PMID: 38780165
قاعدة البيانات: MEDLINE
الوصف
تدمد:1097-4644
DOI:10.1002/jcb.30573