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Functional interaction between nonreceptor tyrosine kinase c-Abl and SR-Rich protein RBM39.

Abstract：

:RBM39, also known as splicing factor HCC1.4, acts as a transcriptional coactivator for the steroid nuclear receptors JUN/AP-1, ESR1/ER-α and ESR2/ER-β. RBM39 is involved in the regulation of the transcriptional responses of these steroid nuclear receptors and promotes transcriptional initiation. In this paper, we report that RBM39 interacts with the nonreceptor tyrosine kinase c-Abl. Both the Src homology (SH) 2 and SH3 domains of c-Abl interact with RBM39. The major tyrosine phosphorylation sites on RBM39 that are phosphorylated by c-Abl are Y95 and Y99, as demonstrated by liquid chromatography coupled with tandem mass spectrometry (LC/MS/MS) and mutational analysis. c-Abl was shown boost the transcriptional coactivation activity of RBM39 for ERα and PRβ in a tyrosine kinase-dependent manner. The results suggest that mammalian c-Abl plays an important role in steroid hormone receptor-mediated transcription by regulating RBM39.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Mai S,Qu X,Li P,Ma Q,Liu X,Cao C

doi

10.1016/j.bbrc.2016.03.108

subject

Has Abstract

pub_date

2016-04-22 00:00:00

pages

355-360

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(16)30421-1

journal_volume

473

pub_type

杂志文章

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