Skip to main content
Log in

Mechanical asymmetry in nucleocytoplasmic protein transport

  • Research Briefing
  • Published:

From Nature Physics

View current issue Submit your manuscript

The nuclear pore complex of eukaryotic cells senses the mechanical directionality of translocating proteins, favouring the passage of those that have a leading mechanically labile region. Adding an unstructured, mechanically weak peptide tag to a translocating protein increases its rate of nuclear import and accumulation, suggesting a biotechnological strategy to enhance the delivery of molecular cargos into the cell nucleus.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1: Mechano-directionality of protein import through the nuclear pore complex (NPC).


  1. Frey, S. et al. Surface properties determining passage rates of proteins through nuclear pores. Cell 174, 202–217 (2018). This paper demonstrates how the chemical properties of the exposed amino acids determine the nucleocytoplasmic transport of proteins.

    Article  Google Scholar 

  2. Infante, E. et al. The mechanical stability of proteins regulates their translocation rate into the cell nucleus. Nat. Phys. 15, 973–981 (2019). This paper explores how the mechanical stability of translocating proteins regulates their import kinetics into the cell nucleus.

    Article  Google Scholar 

  3. Niopek, D., Wehler, P., Roensch, J., Eils, R. & Di Ventura, B. Optogenetic control of nuclear protein export. Nat. Commun. 7, 10624 (2016). This article presents the LEXY probe as a tool for studying nucleocytoplasmic transport.

    Article  ADS  Google Scholar 

  4. Hulsmann, B. B., Labokha, A. A. & Gorlich, D. The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell 150, 738–751 (2012). This paper explores the role of nucleoporins in regulating NPC permeability.

    Article  Google Scholar 

  5. Cordova, J. C. et al. Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine. Cell 158, 647–658 (2014). This paper proves that proteins unfold mechanically upon degradation by ClpXP.

    Article  Google Scholar 

Download references

Additional information

Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

This is a summary of: Panagaki, F. et al. Structural anisotropy results in mechano-directional transport of proteins across nuclear pores. Nat. Phys. (2024).

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Mechanical asymmetry in nucleocytoplasmic protein transport. Nat. Phys. (2024).

Download citation

  • Published:

  • DOI:

  • Springer Nature Limited