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YB‐1 protein: functions and regulation

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Abstract The Y‐box binding protein 1 (YB‐1, YBX1) is a member of the family of DNA‐ and RNA‐binding proteins with an evolutionarily ancient and conserved cold shock domain. It falls into a group of intrinsically disordered proteins that do not follow the classical rule ‘one protein–one function’ but introduce a novel principle stating that a disordered structure suggests many functions. YB‐1 participates in a wide variety of DNA/RNA‐dependent events, including DNA reparation, pre‐mRNA transcription and splicing, mRNA packaging, and regulation of mRNA stability and translation. At the cell level, the multiple activities of YB‐1 are manifested as its involvement in cell proliferation and differentiation, stress response, and malignant cell transformation. WIREs RNA 2014, 5:95–110. doi: 10.1002/wrna.1200 This article is categorized under: RNA Interactions with Proteins and Other Molecules > RNA–Protein Complexes RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications Translation > Translation Regulation

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Domain organization of YB‐1. (1‐50): Disordered Ala/Pro‐rich N‐terminal domain; (51‐128): cold shock domain with a β‐barrel tertiary structure showing low stability in physiological conditions; (129‐324): disordered C‐terminal domain containing alternating clusters of positively and negatively charged amino acid residues. The positions of the nuclear localization signal (NLS), the cytoplasmic retention site (CRS), and the 20S proteasome cleavage site are denoted.
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A scheme of mRNA translational activity as dependent on the YB‐1/mRNA ratio.
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RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications
Translation > Translation Regulation
RNA Interactions with Proteins and Other Molecules > RNA–Protein Complexes

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