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DDX41: a multifunctional DEAD-box protein involved in pre-mRNA splicing and innate immunity

  • Alexandra Z. Andreou ORCID logo EMAIL logo
Veröffentlicht/Copyright: 15. März 2021
Biological Chemistry
Aus der Zeitschrift Biological Chemistry Band 402 Heft 5

Abstract

DEAD-box helicases participate in nearly all steps of an RNA’s life. In recent years, increasing evidence has shown that several family members are multitasking enzymes. They are often involved in different processes, which may be typical for RNA helicases, such as RNA export and translation, or atypical, e.g., acting as nucleic acid sensors that activate downstream innate immune signaling. This review focuses on the DEAD-box protein DDX41 and summarizes our current understanding of its roles as an innate immunity sensor in the cytosol and in pre-mRNA splicing in the nucleus and discusses DDX41’s involvement in disease.

Keywords: acute myeloid leukemia; DEAD-box protein; innate immunity; myelodysplastic syndrome; RNA processing
Corresponding author: Alexandra Z. Andreou, Institute for Physical Chemistry, University of Münster, Corrensstrasse 30, D-48149Münster, Germany, E-mail:

Funding source: Deutsche Forschungsgemeinschaft

Award Identifier / Grant number: AN1138/2-1

Acknowledgments

I would like to thank D. Klostermeier and A. Gubaev for comments on the manuscript. I would also like to thank the reviewers for their constructive comments.

  1. Author contributions: The author has accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: A.Z. Andreou’s work was supported by the Deutsche Forschungsgemeinschaft (AN1138/2-1 to A.Z.A).

  3. Conflict of interest statement: The author declares no conflicts of interest regarding this article.

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Received: 2020-11-18
Accepted: 2021-03-03
Published Online: 2021-03-15
Published in Print: 2021-04-27

© 2021 Walter de Gruyter GmbH, Berlin/Boston

Artikel in diesem Heft

  1. Frontmatter
  2. Highlight: RNA helicases – structure, function, mechanism and regulation
  3. Highlight: RNA helicases – structure, function, mechanism and regulation
  4. Regulation of RNA helicase activity: principles and examples
  5. Regulation of DEAH-box RNA helicases by G-patch proteins
  6. The DEAH helicase DHX36 and its role in G-quadruplex-dependent processes
  7. The DHX36-specific-motif (DSM) enhances specificity by accelerating recruitment of DNA G-quadruplex structures
  8. Mtr4 RNA helicase structures and interactions
  9. Human RecQ helicases in transcription-associated stress management: bridging the gap between DNA and RNA metabolism
  10. Transcription, translation, and DNA repair: new insights from emerging noncanonical substrates of RNA helicases
  11. DDX41: a multifunctional DEAD-box protein involved in pre-mRNA splicing and innate immunity
  12. Dead or alive: DEAD-box ATPases as regulators of ribonucleoprotein complex condensation
https://doi.org/10.1515/hsz-2020-0367
Schlagwörter für diesen Artikel
acute myeloid leukemia; DEAD-box protein; innate immunity; myelodysplastic syndrome; RNA processing

Artikel in diesem Heft

  1. Frontmatter
  2. Highlight: RNA helicases – structure, function, mechanism and regulation
  3. Highlight: RNA helicases – structure, function, mechanism and regulation
  4. Regulation of RNA helicase activity: principles and examples
  5. Regulation of DEAH-box RNA helicases by G-patch proteins
  6. The DEAH helicase DHX36 and its role in G-quadruplex-dependent processes
  7. The DHX36-specific-motif (DSM) enhances specificity by accelerating recruitment of DNA G-quadruplex structures
  8. Mtr4 RNA helicase structures and interactions
  9. Human RecQ helicases in transcription-associated stress management: bridging the gap between DNA and RNA metabolism
  10. Transcription, translation, and DNA repair: new insights from emerging noncanonical substrates of RNA helicases
  11. DDX41: a multifunctional DEAD-box protein involved in pre-mRNA splicing and innate immunity
  12. Dead or alive: DEAD-box ATPases as regulators of ribonucleoprotein complex condensation
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