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Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals.

Fung HY, Fu SC, Chook YM
Elife 6 (2017)
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Cited: 44 times
EuropePMC logo PMID: 28282025

Abstract

Nuclear export receptor CRM1 binds highly variable nuclear export signals (NESs) in hundreds of different cargoes. Previously we have shown that CRM1 binds NESs in both polypeptide orientations (Fung et al., 2015). Here, we show crystal structures of CRM1 bound to eight additional NESs which reveal diverse conformations that range from loop-like to all-helix, which occupy different extents of the invariant NES-binding groove. Analysis of all NES structures show 5-6 distinct backbone conformations where the only conserved secondary structural element is one turn of helix that binds the central portion of the CRM1 groove. All NESs also participate in main chain hydrogen bonding with human CRM1 Lys568 side chain, which acts as a specificity filter that prevents binding of non-NES peptides. The large conformational range of NES backbones explains the lack of a fixed pattern for its 3-5 hydrophobic anchor residues, which in turn explains the large array of peptide sequences that can function as NESs.

Articles - 5uwu mentioned but not cited (3)

  1. Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals. Fung HY, Fu SC, Chook YM. Elife 6 e23961 (2017)
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  8. The Role of Protein Disorder in Nuclear Transport and in Its Subversion by Viruses. Wubben JM, Atkinson SC, Borg NA. Cells 9 E2654 (2020)
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  3. Correlation of CRM1-NES affinity with nuclear export activity. Fu SC, Fung HYJ, Cağatay T, Baumhardt J, Chook YM. Mol Biol Cell 29 2037-2044 (2018)
  4. Nuclear export of ubiquitinated proteins via the UBIN-POST system. Hirayama S, Sugihara M, Morito D, Iemura SI, Natsume T, Murata S, Nagata K. Proc Natl Acad Sci U S A 115 E4199-E4208 (2018)
  5. Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore. Bao XX, Spanos C, Kojidani T, Lynch EM, Rappsilber J, Hiraoka Y, Haraguchi T, Sawin KE. Elife 7 e33465 (2018)
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  15. Using a Simple Cellular Assay to Map NES Motifs in Cancer-Related Proteins, Gain Insight into CRM1-Mediated NES Export, and Search for NES-Harboring Micropeptides. Sendino M, Omaetxebarria MJ, Prieto G, Rodriguez JA. Int J Mol Sci 21 E6341 (2020)
  16. Characterization of Localization and Export Signals of Bovine Torovirus Nucleocapsid Protein Responsible for Extensive Nuclear and Nucleolar Accumulation and Their Importance for Virus Growth. Ujike M, Kawachi Y, Matsunaga Y, Etho Y, Asanuma H, Kamitani W, Taguchi F. J Virol 95 e02111-20 (2021)
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  20. Crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP. Shaikhqasem A, Schmitt K, Valerius O, Ficner R. Acta Crystallogr F Struct Biol Commun 77 70-78 (2021)
  21. Crystallization of Nuclear Export Signals or Small-Molecule Inhibitors Bound to Nuclear Exporter CRM1. Fung HYJ, Chook YM. Methods Mol Biol 2502 285-297 (2022)
  22. Binding Affinity Measurement of Nuclear Export Signal Peptides to Their Exporter CRM1. Fung HYJ, Chook YM. Methods Mol Biol 2502 245-256 (2022)
  23. Characterization of Signal Sequences Determining the Nuclear/Nucleolar Import and Nuclear Export of the Caprine Arthritis-Encephalitis Virus Rev Protein. Labrecque M, Marchand C, Archambault D. Viruses 12 E900 (2020)
  24. DBF4 Dependent Kinase Inhibition Suppresses Hepatocellular Carcinoma Progression and Potentiates Anti-Programmed Cell Death-1 Therapy. Zhang L, Hong J, Chen W, Zhang W, Liu X, Lu J, Tang H, Yang Z, Zhou K, Xie H, Jia C, Jiang D, Zheng S. Int J Biol Sci 19 3412-3427 (2023)
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  26. Karyopherins in the Remodeling of Extracellular Matrix: Implications in Tendon Injury. Diaz C, Thankam FG, Agrawal DK. J Orthop Sports Med 5 357-374 (2023)
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