The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structural and molecular basis of the assembly of the TRPP2/PKD1 complex
Open accessAbstract
Mutations in PKD1 and TRPP2 account for nearly all cases of autosomal dominant polycystic kidney disease (ADPKD). These 2 proteins form a receptor/ion channel complex on the cell surface. Using a combination of biochemistry, crystallography, and a single-molecule method to determine the subunit composition of proteins in the plasma membrane of live cells, we find that this complex contains 3 TRPP2 and 1 PKD1. A newly identified coiled-coil domain in the C terminus of TRPP2 is critical for the formation of this complex. This coiled-coil domain forms a homotrimer, in both solution and crystal structure, and binds to a single coiled-coil domain in the C terminus of PKD1. Mutations that disrupt the TRPP2 coiled-coil domain trimer abolish the assembly of both the full-length TRPP2 trimer and the TRPP2/PKD1 complex and diminish the surface expression of both proteins. These results have significant implications for the assembly, regulation, and function of the TRPP2/PKD1 complex and the pathogenic mechanism of some ADPKD-producing mutations.
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Cites
Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells
Nauli, S. M., Alenghat, F. J., Luo, Y., Williams, E., Vassilev, P., Li, X., Elia, A. E. H., Lu, W., Brown, E. M., Quinn, S. J., et al. (2003) · Nature Genetics · doi:10.1038/ng1076 · Cited by 2,057
The Design of Coiled-Coil Structures and Assemblies
Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585
Parry, D. A. D., Fraser, R. D. B., & Squire, J. M. (2008) · Journal of Structural Biology · doi:10.1016/j.jsb.2008.01.016 · Cited by 264
Cited by
Zhang, M., Ma, Y., Ye, X., Zhang, N., Pan, L., & Wang, B. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01464-x · Cited by 522
Transient receptor potential (TRP) channels: a clinical perspective
Kaneko, Y., & Szallasi, A. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12414 · Cited by 370
Direct recording and molecular identification of the calcium channel of primary cilia
DeCaen, P. G., Delling, M., Vien, T. N., & Clapham, D. E. (2013) · Nature · doi:10.1038/nature12832 · Cited by 306
Structure of the human PKD1-PKD2 complex
Su, Q., Hu, F., Ge, X., Lei, J., Yu, S., Wang, T., Zhou, Q., Mei, C., & Shi, Y. (2018) · Science · doi:10.1126/science.aat9819 · Cited by 284
Polycystin-1 maturation requires polycystin-2 in a dose-dependent manner
Gainullin, V. G., Hopp, K., Ward, C. J., Hommerding, C. J., & Harris, P. C. (2015) · Journal of Clinical Investigation · doi:10.1172/jci76972 · Cited by 135
Metadata
- Authors
- Yu, Y., Ulbrich, M. H., Li, M.-H., Buraei, Z., Chen, X.-Z., Ong, A. C. M., Tong, L., Isacoff, E. Y., & Yang, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-07-14
- Volume
- 106
- Issue
- 28
- Pages
- 11558-11563
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1990405382
- Cited by
- 178
- References
- 3
- FWCI
- 9.09
- Type
- journal article
- Language
- en
- Open access
- green
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- Yu, Y., Ulbrich, M. H., Li, M.-H., Buraei, Z., Chen, X.-Z., Ong, A. C. M., Tong, L., Isacoff, E. Y., & Yang, J. (2009). Structural and molecular basis of the assembly of the TRPP2/PKD1 complex. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0903684106
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