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

Mai, Sanyue; Qu, Xiuhua; Li, Ping; Ma, Qingjun; Liu, Xuan; Cao, Cheng

doi:10.1016/J.BBRC.2016.03.108

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

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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. - Highlights: • c-Abl interacts with RBM39. • RBM39 is phosphorylated by c-Abl. • c-Abl regulates transcriptional coactivation activity of RBM39 on the ERα and PRβ.

Authors:

Mai, Sanyue ^[1]; Qu, Xiuhua ^[2]; Li, Ping; Ma, Qingjun ^[1]; Liu, Xuan ^[1]; Cao, Cheng ^[1]

Beijing Institute of Biotechnology, 27 Taiping Rd, Haidian District, Beijing 100850 (China)
General Navy Hospital of PLA, 6 Fucheng Rd, Haidian District, Beijing 100037 (China)

Publication Date:: Fri Apr 22 00:00:00 EDT 2016

OSTI Identifier:: 22596355

Resource Type:: Journal Article

Journal Name:: Biochemical and Biophysical Research Communications

Additional Journal Information:: Journal Volume: 473; Journal Issue: 1; Other Information: Copyright (c) 2016 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X

Country of Publication:: United States

Language:: English

Subject:: 60 APPLIED LIFE SCIENCES; ARGININE; CATTLE; CHEMILUMINESCENCE; ESTROGENS; FIBROBLASTS; GLUTATHIONE; LIQUID COLUMN CHROMATOGRAPHY; MASS SPECTROSCOPY; PHOSPHORYLATION; PROGESTERONE; RECEPTORS; RNA; SERINE; TRANSFERASES; TYROSINE

Citation Formats


                    Mai, Sanyue, Qu, Xiuhua, Li, Ping, Ma, Qingjun, Liu, Xuan, and Cao, Cheng. Functional interaction between nonreceptor tyrosine kinase c-Abl and SR-Rich protein RBM39.  United States: N. p., 2016. 
        Web.  doi:10.1016/J.BBRC.2016.03.108.

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                    Mai, Sanyue, Qu, Xiuhua, Li, Ping, Ma, Qingjun, Liu, Xuan, & Cao, Cheng. Functional interaction between nonreceptor tyrosine kinase c-Abl and SR-Rich protein RBM39.  United States.  https://doi.org/10.1016/J.BBRC.2016.03.108

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                    Mai, Sanyue, Qu, Xiuhua, Li, Ping, Ma, Qingjun, Liu, Xuan, and Cao, Cheng. 2016.  
        "Functional interaction between nonreceptor tyrosine kinase c-Abl and SR-Rich protein RBM39".  United States.  https://doi.org/10.1016/J.BBRC.2016.03.108.

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@article{osti_22596355,

  title        = {Functional interaction between nonreceptor tyrosine kinase c-Abl and SR-Rich protein RBM39},

  author       = {Mai, Sanyue and Qu, Xiuhua and Li, Ping and Ma, Qingjun and Liu, Xuan and Cao, Cheng},

  abstractNote = {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. - Highlights: • c-Abl interacts with RBM39. • RBM39 is phosphorylated by c-Abl. • c-Abl regulates transcriptional coactivation activity of RBM39 on the ERα and PRβ.},

  doi          = {10.1016/J.BBRC.2016.03.108},

  url          = {https://www.osti.gov/biblio/22596355},
  journal      = {Biochemical and Biophysical Research Communications},

  issn         = {0006-291X},

  number       = 1,

  volume       = 473,

  place        = {United States},

  year         = {Fri Apr 22 00:00:00 EDT 2016},

  month        = {Fri Apr 22 00:00:00 EDT 2016}

}

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