Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain - Université d'Évry Access content directly
Journal Articles Communications Biology Year : 2021

Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain

Hélène Henrie
  • Function : Author
Nicolas Babault
  • Function : Author
Pierrick Craveur
  • Function : Author

Abstract

The RNA-binding protein Lin28 (Lin28a) is an important pluripotency factor that reprograms translation and promotes cancer progression. Although Lin28 blocks let-7 microRNA maturation, Lin28 also binds to a large set of cytoplasmic mRNAs directly. However, how Lin28 regulates the processing of many mRNAs to reprogram global translation remains unknown. We show here, using a structural and cellular approach, a mixing of Lin28 with YB-1 (YBX1) in the presence of mRNA owing to their cold-shock domain, a conserved β-barrel structure that binds to ssRNA cooperatively. In contrast, the other RNA binding-proteins without cold-shock domains tested, HuR, G3BP-1, FUS and LARP-6, did not mix with YB-1. Given that YB-1 is the core component of dormant mRNPs, a model in which Lin28 gains access to mRNPs through its co-association with YB-1 to mRNA may provide a means for Lin28 to reprogram translation. We anticipate that the translational plasticity provided by mRNPs may contribute to Lin28 functions in development and adaptation of cancer cells to an adverse environment.
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Dates and versions

hal-03176308 , version 1 (22-03-2021)

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Anastasiia Samsonova, Krystel El Hage, Bénédicte Desforges, Vandana Joshi, Marie-Jeanne Clément, et al.. Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain. Communications Biology, 2021, 4 (1), pp.359. ⟨10.1038/s42003-021-01862-3⟩. ⟨hal-03176308⟩
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