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Toward Unraveling Molecular Grammars for dsRNA-binding Proteins: Substrate Recognition to Binding Mechanisms

  • 작성자

    Yoosik Kim
  • 작성일자

    2025-11-21
  • 조회수

    377
Name: Yoosik Kim ( ysyoosik@kaist.ac.kr )
2021-presentAssociate Professor, Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology, South Korea
2016-2021Assistant Professor, Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology, South Korea
2011-2015Postdoctoral research fellow, Seoul National University, South Korea
2006-2011Ph.D., Department of Chemical and Biological Engineering, Princeton University, USA

Toward Unraveling Molecular Grammars for dsRNA-binding Proteins: Substrate Recognition to Binding Mechanisms

Long double-stranded RNAs (dsRNAs) and recognized by innate immune response proteins, initiating integrated stress response in cells. As these RNAs adopt an A-form helical structure, immune sensors recognize dsRNAs primarily based on the structural features, such as the length of the double-stranded stretch, rather than specific sequences. Moreover, this structure-dependent, sequence-independent protein-RNA mode of recognition also applies to other dsRNA-binding proteins (dsRBPs). As a result, multiple dsRBPs share a common pool of dsRNA substrates, creating a complex network of dsRBPs in which these proteins influence the activation status and signaling activity of each other. With the advent of advanced analytical techniques capable of studying RNA sequences and structures at single-nucleotide resolution, studies have begun to explore dsRNA-protein interactions in greater details. In this review, we summarize the dsRBPs encoded in the human genome, their RNA substrates and recognition mechanisms, and the downstream effects of protein-RNA interactions, aiming to deepen our understanding of dsRNA recognition and signaling.