The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly
Open accessAbstract
Bardet-Biedl syndrome (BBS) is a human genetic disorder resulting in obesity, retinal degeneration, polydactyly, and nephropathy. Recent studies indicate that trafficking defects to the ciliary membrane are involved in this syndrome. Here, we show that a novel complex composed of three chaperonin-like BBS proteins (BBS6, BBS10, and BBS12) and CCT/TRiC family chaperonins mediates BBSome assembly, which transports vesicles to the cilia. Chaperonin-like BBS proteins interact with a subset of BBSome subunits and promote their association with CCT chaperonins. CCT activity is essential for BBSome assembly, and knockdown of CCT chaperonins in zebrafish results in BBS phenotypes. Many disease-causing mutations found in BBS6, BBS10, and BBS12 disrupt interactions among these BBS proteins. Our data demonstrate that BBS6, BBS10, and BBS12 are necessary for BBSome assembly, and that impaired BBSome assembly contributes to the etiology of BBS phenotypes associated with the loss of function of these three BBS genes.
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Nachury, M. V., Loktev, A. V., Zhang, Q., Westlake, C. J., Peränen, J., Merdes, A., Slusarski, D. C., Scheller, R. H., Bazan, J. F., Sheffield, V. C., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.053 · Cited by 1,384
Self-citationBerbari, N. F., Lewis, J. S., Bishop, G. A., Askwith, C. C., & Mykytyn, K. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711027105 · Cited by 474
The proteome of the mouse photoreceptor sensory cilium complex
Liu, Q., Tan, G., Levenkova, N., Li, T., Pugh, E. N., Rux, J. J., Speicher, D. W., & Pierce, E. A. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700054-mcp200 · Cited by 359
Marion, V., Stoetzel, C., Schlicht, D., Messaddeq, N., Koch, M., Flori, E., Danse, J. M., Mandel, J.-L., & Dollfus, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812518106 · Cited by 178
Cited by
Signaling through the Primary Cilium
Wheway, G., Nazlamova, L., & Hancock, J. T. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00008 · Cited by 483
An organelle-specific protein landscape identifies novel diseases and molecular mechanisms
Boldt, K., van Reeuwijk, J., Lu, Q., Koutroumpas, K., Nguyen, T.-M. T., Texier, Y., van Beersum, S. E. C., Horn, N., Willer, J. R., Mans, D. A., et al. (2016) · Nature Communications · doi:10.1038/ncomms11491 · Cited by 240
The roles of evolutionarily conserved functional modules in cilia-related trafficking
Sung, C.-H., & Leroux, M. R. (2013) · Nature Cell Biology · doi:10.1038/ncb2888 · Cited by 186
Trafficking of ciliary membrane proteins by the intraflagellar transport/BBSome machinery
Wingfield, J. L., Lechtreck, K.-F., & Lorentzen, E. (2018) · Essays in Biochemistry · doi:10.1042/ebc20180030 · Cited by 157
The role of primary cilia in the development and disease of the retina
Wheway, G., Parry, D. A., & Johnson, C. A. (2014) · Organogenesis · doi:10.4161/org.26710 · Cited by 152
Metadata
- Authors
- Seo, S., Baye, L. M., Schulz, N. P., Beck, J. S., Zhang, Q., Slusarski, D. C., & Sheffield, V. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-01-06
- Volume
- 107
- Issue
- 4
- Pages
- 1488-1493
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2137418427
- Cited by
- 324
- References
- 4
- FWCI
- 13.08
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly. https://app.cochat.ai/papers/10.1073/pnas.0910268107
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- Seo, S., Baye, L. M., Schulz, N. P., Beck, J. S., Zhang, Q., Slusarski, D. C., & Sheffield, V. C. (2010). BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0910268107
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