دورية أكاديمية
Enhancer of rudimentary homologue interacts with scaffold attachment factor B at the nuclear matrix to regulate SR protein phosphorylation
| العنوان: | Enhancer of rudimentary homologue interacts with scaffold attachment factor B at the nuclear matrix to regulate SR protein phosphorylation |
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| المؤلفون: | Drakouli S., Lyberopoulou A., Papathanassiou M., Mylonis I., Georgatsou E. |
| المصدر: | FEBS Journal ; https://www.scopus.com/inward/record.uri?eid=2-s2.0-85021884636&doi=10.1111%2ffebs.14141&partnerID=40&md5=4f771c2559845b409aba6b723bd4fa3fTest |
| سنة النشر: | 2017 |
| المجموعة: | University of Thessaly Institutional Repository / Ιδρυματικό Αποθετήριο Πανεπιστημίου Θεσσαλίας |
| مصطلحات موضوعية: | estrogen receptor alpha, serine arginine rich protein, cell cycle protein, ERH protein, human, estrogen receptor, green fluorescent protein, hybrid protein, matrix attachment region binding protein, nuclear matrix protein, peptide fragment, protein serine threonine kinase, SAFB protein, SAFB2 protein, serine arginine rich splicing factor, SRPK1 protein, transcription factor, Article, carboxy terminal sequence, cell nucleus matrix, controlled study, ERH gene, gene function, gene interaction, gene location, gene silencing, genetic transcription, human cell, in vitro study, priority journal |
| الوصف: | Scaffold attachment factor B1 (SAFB1) is an integral component of the nuclear matrix of vertebrate cells. It binds to DNA on scaffold/matrix attachment region elements, as well as to RNA and a multitude of different proteins, affecting basic cellular activities such as transcription, splicing and DNA damage repair. In the present study, we show that enhancer of rudimentary homologue (ERH) is a new molecular partner of SAFB1 and its 70% homologous paralogue, scaffold attachment factor B2 (SAFB2). ERH interacts directly in the nucleus with the C-terminal Arg-Gly-rich region of SAFB1/2 and co-localizes with it in the insoluble nuclear fraction. ERH, a small ubiquitous protein with striking homology among species and a unique structure, has also been implicated in fundamental cellular mechanisms. Our functional analyses suggest that the SAFB/ERH interaction does not affect SAFB1/2 function in transcription (e.g. as oestrogen receptor α co-repressors), although it reverses the inhibition exerted by SAFB1/2 on the splicing kinase SR protein kinase 1 (SRPK1), which also binds on the C-terminus of SAFB1/2. Accordingly, ERH silencing decreases lamin B receptor and SR protein phosphorylation, which are major SRPK1 substrates, further substantiating the role of SAFB1 and SAFB2 in the co-ordination of nuclear function. © 2017 Federation of European Biochemical Societies |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1742464X |
| العلاقة: | http://hdl.handle.net/11615/71212Test |
| DOI: | 10.1111/febs.14141 |
| الإتاحة: | https://doi.org/10.1111/febs.14141Test http://hdl.handle.net/11615/71212Test |
| رقم الانضمام: | edsbas.7F154121 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 1742464X |
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| DOI: | 10.1111/febs.14141 |