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SRSF3 Is a Critical Requirement for Inclusion of Exon 3 of BIS Pre-mRNA.
Baek, Ji-Ye; Yun, Hye-Hyeon; Jung, Soon-Young; Lee, Jeehan; Yoo, Kyunghyun; Lee, Jeong-Hwa.
Afiliação
  • Baek JY; Department of Biochemistry, The Catholic University of Korea, 222, Banpo-daero, Seocho-gu, Seoul 06591, Korea.
  • Yun HH; Institute of Aging and Metabolic Diseases, College of Medicine, The Catholic University of Korea, 222, Banpo-daero, Seocho-gu, Seoul 06591, Korea.
  • Jung SY; Department of Biomedicine & Health Sciences, College of Medicine, The Catholic University of Korea, 222, Banpo-daero, Seocho-gu, Seoul 06591, Korea.
  • Lee J; Department of Biochemistry, The Catholic University of Korea, 222, Banpo-daero, Seocho-gu, Seoul 06591, Korea.
  • Yoo K; Institute of Aging and Metabolic Diseases, College of Medicine, The Catholic University of Korea, 222, Banpo-daero, Seocho-gu, Seoul 06591, Korea.
  • Lee JH; Department of Biochemistry, The Catholic University of Korea, 222, Banpo-daero, Seocho-gu, Seoul 06591, Korea.
Cells ; 9(10)2020 10 19.
Article em En | MEDLINE | ID: mdl-33086735
BCL-2 interacting cell death suppressor (BIS), also known as BAG3, is a multifunctional protein. Aberrant expression and mutation of BIS have been implicated in cancers and myopathy. However, there have only been a few studies on the splicing of BIS pre-mRNA. In the present study, through RT-PCR and sequencing in various cell lines and mouse tissues, we identified for the first time the presence of BIS mRNA isomers in which exon 3 or exons 2-3 are skipped. We also demonstrated that the depletion of SRSF3 promoted the skipping of exon 3 of BIS pre-mRNA in endogenous BIS and the GFP-BIS minigene. SRSF3 specifically interacts with the putative binding sites in exon 3, in which deletion promoted the skipping of exon 3 in the GFP-BIS minigene, which was comparable to the effect of SRSF knockdown. Even though acceleration of exon 3 skipping was not observed in response to various stimuli, SRSF3 depletion, accompanied by the production of a truncated BIS protein, inhibited the nuclear translocation of HSF1, which was restored by the wild-type BIS, not by exon 3-depleted BIS. Therefore, our results suggested that the maintenance of SRSF3 levels and subsequent preservation of the intact BIS protein is an important factor in modulating HSF1 localization upon cellular stress.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Precursores de RNA / Éxons / Proteínas Adaptadoras de Transdução de Sinal / Proteínas Reguladoras de Apoptose / Fatores de Processamento de Serina-Arginina Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Revista: Cells Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Precursores de RNA / Éxons / Proteínas Adaptadoras de Transdução de Sinal / Proteínas Reguladoras de Apoptose / Fatores de Processamento de Serina-Arginina Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Revista: Cells Ano de publicação: 2020 Tipo de documento: Article