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Distinct mechanisms obviate the potentially toxic effects of inverted-repeat Alu elements on cellular RNA metabolism

Nature Structural & Molecular Biology volume 24, pages 496–498 (2017)Cite this article

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Two new studies show that RNA-binding proteins can mediate distinct and beneficial effects to cells by binding to the extensive double-stranded RNA (dsRNA) structures of inverted-repeat Alu elements (IRAlus). One study reports stress-induced export of the 110-kDa isoform of the adenosine deaminase acting on RNA 1 protein (ADAR1p110) to the cytoplasm, where it binds IRAlus so as to protect many mRNAs encoding anti-apoptotic proteins from degradation. The other study demonstrates that binding of the nuclear helicase DHX9 to IRAlus embedded within RNAs minimizes defects in RNA processing.

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Figure 1: ADAR mediates A-to-I editing so as to destabilize cellular double-stranded RNA structures.

Debbie Maizels/Springer Nature

Figure 2: Export of nuclear ADAR1p110 to the cytoplasm protects cells from apoptosis triggered by 3′-UTR IRAlus.

Debbie Maizels/Springer Nature

Figure 3: The nuclear helicase DHX9 binds intronic IRAlus to suppress defective RNA processing.

Debbie Maizels/Springer Nature

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Acknowledgements

The authors thank M. Popp for critically reading this submission. Work in the Maquat lab on Alu elements is supported by NIH grant R37 GM074593 to L.E.M.

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Authors and Affiliations

  1. Reyad A. Elbarbary and Lynne E. Maquat are in the Department of Biochemistry and Biophysics, School of Medicine and Dentistry, and Center for RNA Biology, University of Rochester, Rochester, New York, USA.,

    Reyad A Elbarbary & Lynne E Maquat

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  1. Reyad A Elbarbary
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  2. Lynne E Maquat
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Correspondence to Reyad A Elbarbary or Lynne E Maquat.

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Elbarbary, R., Maquat, L. Distinct mechanisms obviate the potentially toxic effects of inverted-repeat Alu elements on cellular RNA metabolism. Nat Struct Mol Biol 24, 496–498 (2017). https://doi.org/10.1038/nsmb.3416

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