HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs

@inproceedings{Pabis2019HuRBF,
  title={HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs},
  author={Marta Pabis and G M Popowicz and Ralf Stehle and David Fern{\'a}ndez-Ramos and Sam Asami and Lisa A. Warner and Sof{\'i}a Mu{\~n}oz Garc{\'i}a-Mauri{\~n}o and Andreas Schlundt and Mar{\'i}a L. Mart{\'i}nez-Chantar and Irene D{\'i}az-Moreno and Michael Sattler},
  booktitle={Nucleic acids research},
  year={2019}
}
HuR/ELAVL1 is an RNA-binding protein involved in differentiation and stress response that acts primarily by stabilizing messenger RNA (mRNA) targets. HuR comprises three RNA recognition motifs (RRMs) where the structure and RNA binding of RRM3 and of full-length HuR remain poorly understood. Here, we report crystal structures of RRM3 free and bound to cognate RNAs. Our structural, NMR and biochemical data show that RRM3 mediates canonical RNA interactions and reveal molecular details of a… CONTINUE READING
6
Twitter Mentions

Similar Papers

Citations

Publications citing this paper.

References

Publications referenced by this paper.
SHOWING 1-10 OF 72 REFERENCES

The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets

R. M. Scheiba, A. I. de Opakua, +5 authors I. Diaz-Moreno
  • RNA Biol.,
  • 2014
VIEW 8 EXCERPTS
HIGHLY INFLUENTIAL

The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding.

  • Acta crystallographica. Section D, Biological crystallography
  • 2013
VIEW 5 EXCERPTS
HIGHLY INFLUENTIAL

Identification of a target RNA motif for RNA-binding protein

I. Lopez de Silanes, M. Zhan, A. Lal, X. Yang, M. Gorospe
  • HuR. PNAS,
  • 2004
VIEW 3 EXCERPTS
HIGHLY INFLUENTIAL