The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport
Open accessAbstract
Natively unfolded phenylalanine-glycine (FG)-repeat domains are alleged to form the physical constituents of the selective barrier-gate in nuclear pore complexes during nucleocytoplasmic transport. Presently, the biophysical mechanism behind the selective gate remains speculative because of a lack of information regarding the nanomechanical properties of the FG domains. In this work, we have applied the atomic force microscope to measure the mechanical response of individual and clusters of FG molecules. Single-molecule force spectroscopy reveals that FG molecules are unfolded and highly flexible. To provide insight into the selective gating mechanism, an experimental platform has been constructed to study the collective behavior of surface-tethered FG molecules at the nanoscale. Measurements indicate that the collective behavior of such FG molecules gives rise to an exponentially decaying long-range steric repulsive force. This finding indicates that the molecules are thermally mobile in an extended polymer brush-like conformation. This assertion is confirmed by observing that the brush-like conformation undergoes a reversible collapse transition in less polar solvent conditions. These findings reveal how FG-repeat domains may simultaneously function as an entropic barrier and a selective trap in the near-field interaction zone of nuclear pore complexes; i.e., selective gate.
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Cited by
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Natively Unfolded Nucleoporins Gate Protein Diffusion across the Nuclear Pore Complex
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Integrative structure and functional anatomy of a nuclear pore complex
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Nanomechanical Basis of Selective Gating by the Nuclear Pore Complex
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Metadata
- Authors
- Lim, R. Y. H., Huang, N.-P., Köser, J., Deng, J., Lau, K. H. A., Schwarz-Herion, K., Fahrenkrog, B., & Aebi, U.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-06-20
- Volume
- 103
- Issue
- 25
- Pages
- 9512-9517
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2020415369
- Cited by
- 273
- References
- 41
- FWCI
- 7.61
- Type
- journal article
- Language
- en
- Open access
- green
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