Journalartikel

Jahr der Veröffentlichung: 2012

Seiten: 8622-8636

Zeitschrift: Nucleic Acids Research

Bandnummer: 40

Heftnummer: 17

ISSN: 0305-1048

eISSN: 1362-4962

Open Access Status: Gold

DOI Link: https://doi.org/10.1093/nar/gks579

Verlag: Oxford University Press

Abstract: 
The human Y box-binding protein-1 (YB-1) is a deoxyribonucleic acid (DNA)/ribonucleic acid (RNA)-binding protein with pleiotropic functions. Besides its roles in the regulation of transcription and translation, several recent studies indicate that YB-1 is a spliceosome-associated protein and is involved in alternative splicing, but the underlying mechanism has remained elusive. Here, we define both CAUC and CACC as high-affinity binding motifs for YB-1 by systematic evolution of ligands by exponential enrichment (SELEX) and demonstrate that these newly defined motifs function as splicing enhancers. Interestingly, on the endogenous CD44 gene, YB-1 appears to mediate a network interaction to activate exon v5 inclusion via multiple CAUC motifs in both the alternative exon and its upstream polypyrimidine tract. We provide evidence that YB-1 activates splicing by facilitating the recruitment of U2AF65 to weak polypyrimidine tracts through direct protein-protein interactions. Together, these findings suggest a vital role of YB-1 in activating a subset of weak 3' splice sites in mammalian cells.

Harvard-Zitierstil: Wei, W., Mu, S., Heiner, M., Fu, X., Cao, L., Gong, X., et al. (2012) YB-1 binds to CAUC motifs and stimulates exon inclusion by enhancing the recruitment of U2AF to weak polypyrimidine tracts, Nucleic Acids Research, 40(17), pp. 8622-8636. https://doi.org/10.1093/nar/gks579

APA-Zitierstil: Wei, W., Mu, S., Heiner, M., Fu, X., Cao, L., Gong, X., Bindereif, A., & Hui, J. (2012). YB-1 binds to CAUC motifs and stimulates exon inclusion by enhancing the recruitment of U2AF to weak polypyrimidine tracts. Nucleic Acids Research. 40(17), 8622-8636. https://doi.org/10.1093/nar/gks579