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Enhancer of rudimentary homologue interacts with scaffold attachment factor B at the nuclear matrix to regulate SR protein phosphorylation
Author(s) -
Drakouli Sotiria,
Lyberopoulou Aggeliki,
Papathanassiou Maria,
Mylonis Ilias,
Georgatsou Eleni
Publication year - 2017
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14141
Subject(s) - enhancer , scaffold protein , microbiology and biotechnology , nuclear matrix , phosphorylation , transcription factor , scaffold/matrix attachment region , biology , rna splicing , nuclear protein , chemistry , dna , signal transduction , chromatin , genetics , rna , chromatin remodeling , gene
Scaffold attachment factor B1 ( SAFB 1) 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 SAFB 1 and its 70% homologous paralogue, scaffold attachment factor B2 ( SAFB 2). ERH interacts directly in the nucleus with the C‐terminal Arg‐Gly‐rich region of SAFB 1/2 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 SAFB 1/2 function in transcription (e.g. as oestrogen receptor α co‐repressors), although it reverses the inhibition exerted by SAFB 1/2 on the splicing kinase SR protein kinase 1 ( SRPK 1), which also binds on the C‐terminus of SAFB 1/2. Accordingly, ERH silencing decreases lamin B receptor and SR protein phosphorylation, which are major SRPK 1 substrates, further substantiating the role of SAFB 1 and SAFB 2 in the co‐ordination of nuclear function.