The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
Open accessAbstract
Nuclear transport proceeds through nuclear pore complexes (NPCs) that are embedded in the nuclear envelope of eukaryotic cells. The Saccharomyces cerevisiae NPC is comprised of 30 nucleoporins (Nups), 13 of which contain phenylalanine-glycine repeats (FG Nups) that bind karyopherins and facilitate the transport of karyopherin-cargo complexes. Here, we characterize the structural properties of S. cerevisiae FG Nups by using biophysical methods and predictive amino acid sequence analyses. We find that FG Nups, particularly the large FG repeat regions, exhibit structural characteristics typical of “natively unfolded” proteins (highly flexible proteins that lack ordered secondary structure). Furthermore, we use protease sensitivity assays to demonstrate that most FG Nups are disordered in situ within the NPCs of purified yeast nuclei. The conclusion that FG Nups constitute a family of natively unfolded proteins supports the hypothesis that the FG repeat regions of Nups form a meshwork of random coils at the NPC through which nuclear transport proceeds.
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Cites
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Siegel, L. M., & Monty, K. J. (1966) · Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis · doi:10.1016/0926-6585(66)90333-5 · Cited by 2,226
Why are ?natively unfolded? proteins unstructured under physiologic conditions?
Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000) · Proteins: Structure, Function, and Genetics · doi:10.1002/1097-0134(20001115)41:3<415::aid-prot130>3.0.co;2-7 · Cited by 2,078
Self-citationTransport Between the Cell Nucleus and the Cytoplasm
Görlich, D., & Kutay, U. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.607 · Cited by 2,022
Natively unfolded proteins: A point where biology waits for physics
Uversky, V. N. (2002) · Protein Science · doi:10.1110/ps.4210102 · Cited by 1,813
Self-citationIntrinsically Disordered Proteins
Uversky, V. N. (2013) · Brenner's Encyclopedia of Genetics · doi:10.1016/b978-0-12-374984-0.01698-3 · Cited by 1,637
Self-citationThe Yeast Nuclear Pore Complex
Rout, M. P., Aitchison, J. D., Suprapto, A., Hjertaas, K., Zhao, Y., & Chait, B. T. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.4.635 · Cited by 1,400
Coupling of folding and binding for unstructured proteins
Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327
What does it mean to be natively unfolded?
Uversky, V. N. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02649.x · Cited by 982
Self-citationTransport into and out of the Nucleus
Macara, I. G. (2001) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.65.4.570-594.2001 · Cited by 905
Cited by
Molecular mechanism of the nuclear protein import cycle
Stewart, M. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2114 · Cited by 919
The interplay between structure and function in intrinsically unstructured proteins
Tompa, P. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.072 · Cited by 717
Frey, S., Richter, R. P., & Görlich, D. (2006) · Science · doi:10.1126/science.1132516 · Cited by 688
A Saturated FG-Repeat Hydrogel Can Reproduce the Permeability Properties of Nuclear Pore Complexes
Frey, S., & Görlich, D. (2007) · Cell · doi:10.1016/j.cell.2007.06.024 · Cited by 567
Probing nuclear pore complex architecture with proximity-dependent biotinylation
Kim, D. I., KC, B., Zhu, W., Motamedchaboki, K., Doye, V., & Roux, K. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406459111 · Cited by 560
Metadata
- Authors
- Denning, D. P., Patel, S. S., Uversky, V., Fink, A. L., & Rexach, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-02-25
- Volume
- 100
- Issue
- 5
- Pages
- 2450-2455
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2150359450
- Cited by
- 503
- References
- 31
- FWCI
- 6.76
- Type
- journal article
- Language
- en
- Open access
- green
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- Denning, D. P., Patel, S. S., Uversky, V., Fink, A. L., & Rexach, M. (2003). Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0437902100
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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