Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain
Samsonova et al. show a cooperative association of Lin28 and YB-1 for their target mRNA through their cold-shock domain, which is a conserved β-barrel structure that binds to single-stranded RNA. This study suggests that the association of Lin28 with YB-1 in mRNPs may contribute to the translational...
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| Autores principales: | , , , , , , , , , , , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/15258b4c3a3942419e49124926949c3e |
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| Sumario: | Samsonova et al. show a cooperative association of Lin28 and YB-1 for their target mRNA through their cold-shock domain, which is a conserved β-barrel structure that binds to single-stranded RNA. This study suggests that the association of Lin28 with YB-1 in mRNPs may contribute to the translational plasticity during development and the adaptation of cancer cells to adverse environments. |
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