The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Interaction between RGS7 and polycystin
Open accessAbstract
Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase activity of certain Gα subunits and thereby modulate a number of G protein-dependent signaling cascades. Currently, little is known about the regulation of RGS proteins themselves. We identified a short-lived RGS protein, RGS7, that is rapidly degraded through the proteasome pathway. The degradation of RGS7 is inhibited by interaction with a C-terminal domain of polycystin, the protein encoded by PKD1 , a gene involved in autosomal-dominant polycystic kidney disease. Furthermore, membranous expression of C-terminal polycystin relocalized RGS7. Our results indicate that rapid degradation and interaction with integral membrane proteins are potential means of regulating RGS proteins.
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The N-end rule: functions, mysteries, uses
Varshavsky, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12142 · Cited by 859
Cited by
Autosomal dominant polycystic kidney disease
Torres, V. E., Harris, P. C., & Pirson, Y. (2007) · The Lancet · doi:10.1016/s0140-6736(07)60601-1 · Cited by 1,550
Genetics and Pathogenesis of Polycystic Kidney Disease
Igarashi, P., & Somlo, S. (2002) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000028643.17901.42 · Cited by 593
Metadata
- Authors
- Kim, E., Arnould, T., Sellin, L., Benzing, T., Comella, N., Kocher, O., Tsiokas, L., Sukhatme, V. P., & Walz, G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1999-05-25
- Volume
- 96
- Issue
- 11
- Pages
- 6371-6376
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1975792086
- Cited by
- 163
- References
- 1
- FWCI
- 5.98
- Type
- journal article
- Language
- en
- Open access
- green
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- Kim, E., Arnould, T., Sellin, L., Benzing, T., Comella, N., Kocher, O., Tsiokas, L., Sukhatme, V. P., & Walz, G. (1999). Interaction between RGS7 and polycystin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.11.6371
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