4.7 Review

Emerging molecular functions and novel roles for the DEAD-box protein Dbp5/DDX19 in gene expression

Journal

CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 78, Issue 5, Pages 2019-2030

Publisher

SPRINGER BASEL AG
DOI: 10.1007/s00018-020-03680-y

Keywords

DBP5; DDX19; GLE1; NUP159; Nuclear pore complex; mRNA export; Gene expression; mRNP; RNPase

Funding

  1. predoctoral Training Program in Molecular and Cellular Biology at UC Davis - NIH T32 training grant [GM007377]
  2. National Institute of General Medical Sciences of the National Institutes of Health [R01GM124120]

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The DEAD-box protein Dbp5 is a member of the SFII helicase superfamily and plays multiple important roles in gene expression, including regulating mRNA export, non-coding RNA export, translation, transcription, and DNA metabolism. It has the ability to function in different cellular compartments and modulate various stages of RNA lifecycle. Despite over 20 years of research on Dbp5, unanswered questions remain regarding its localization, substrate selection, and mechanistic principles in gene expression.
The DEAD-box protein (DBP) Dbp5, a member of the superfamily II (SFII) helicases, has multiple reported roles in gene expression. First identified as an essential regulator of mRNA export in Saccharomyces cerevisiae, the enzyme now has reported functions in non-coding RNA export, translation, transcription, and DNA metabolism. Localization of the protein to various cellular compartments (nucleoplasm, nuclear envelope, and cytoplasm) highlights the ability of Dbp5 to modulate different stages of the RNA lifecycle. While Dbp5 has been well studied for>20 years, several critical questions remain regarding the mechanistic principles that govern Dbp5 localization, substrate selection, and functions in gene expression. This review aims to take a holistic view of the proposed functions of Dbp5 and evaluate models that accommodate current published data.

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