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Rbfox Proteins Regulate Splicing as Part of a Large Multiprotein Complex LASR.
Damianov, Andrey; Ying, Yi; Lin, Chia-Ho; Lee, Ji-Ann; Tran, Diana; Vashisht, Ajay A; Bahrami-Samani, Emad; Xing, Yi; Martin, Kelsey C; Wohlschlegel, James A; Black, Douglas L.
Afiliación
  • Damianov A; Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Ying Y; Molecular Biology Interdepartmental Ph.D. Program, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Lin CH; Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Lee JA; Department of Biological Chemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Tran D; Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Vashisht AA; Department of Biological Chemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Bahrami-Samani E; Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Xing Y; Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Martin KC; Department of Biological Chemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Wohlschlegel JA; Department of Biological Chemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Black DL; Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095, USA. Electronic address: dougb@microbio.ucla.edu.
Cell ; 165(3): 606-19, 2016 Apr 21.
Article en En | MEDLINE | ID: mdl-27104978
ABSTRACT
Rbfox proteins control alternative splicing and posttranscriptional regulation in mammalian brain and are implicated in neurological disease. These proteins recognize the RNA sequence (U)GCAUG, but their structures and diverse roles imply a variety of protein-protein interactions. We find that nuclear Rbfox proteins are bound within a large assembly of splicing regulators (LASR), a multimeric complex containing the proteins hnRNP M, hnRNP H, hnRNP C, Matrin3, NF110/NFAR-2, NF45, and DDX5, all approximately equimolar to Rbfox. We show that splicing repression mediated by hnRNP M is stimulated by Rbfox. Virtually all the intron-bound Rbfox is associated with LASR, and hnRNP M motifs are enriched adjacent to Rbfox crosslinking sites in vivo. These findings demonstrate that Rbfox proteins bind RNA with a defined set of cofactors and affect a broader set of exons than previously recognized. The function of this multimeric LASR complex has implications for deciphering the regulatory codes controlling splicing networks.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Empalme del ARN / Proteínas de Unión al ARN Límite: Animals / Humans Idioma: En Revista: Cell Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Empalme del ARN / Proteínas de Unión al ARN Límite: Animals / Humans Idioma: En Revista: Cell Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos