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14-3-3 Proteins Modulate the Expression of Epithelial Na+ Channels by Phosphorylation-dependent Interaction with Nedd4-2 Ubiquitin Ligase
Open accessAbstract
The ubiquitin E3 protein ligase Nedd4-2 is a physiological regulator of the epithelial sodium channel ENaC, which is essential for transepithelial Na+ transport and is linked to Liddle's syndrome, an autosomal dominant disorder of human salt-sensitive hypertension. Nedd4-2 function is negatively regulated by phosphorylation via a serum- and glucocorticoid-inducible protein kinase (Sgk1), which serves as a mechanism to inhibit the ubiquitination-dependent degradation of ENaC. We report here that 14-3-3 proteins participate in this regulatory process through a direct interaction with a phosphorylated form of human Nedd4-2 (a human gene product of KIAA0439, termed hNedd4-2). The interaction is dependent on Sgk1-catalyzed phosphorylation of hNedd4-2 at Ser-468. We found that this interaction preserved the activity of the Sgk1-stimulated ENaC-dependent Na+ current while disrupting the interaction decreased ENaC density on the Xenopus laevis oocytes surface possibly by enhancing Nedd4-2-mediated ubiquitination that leads to ENaC degradation. Our findings suggest that 14-3-3 proteins modulate the cell surface density of ENaC cooperatively with Sgk1 kinase by maintaining hNedd4-2 in an inactive phosphorylated state.
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Chang, S. S., Grunder, S., Hanukoglu, A., Rösler, A., Mathew, P. M., Hanukoglu, I., Schild, L., Lu, Y., Shimkets, R. A., Nelson-Williams, C., et al. (1996) · Nature Genetics · doi:10.1038/ng0396-248 · Cited by 808
The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
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Phosphorylation of Nedd4‐2 by Sgk1 regulates epithelial Na+ channel cell surface expression
Debonneville, C., Flores, S. Y., Kamynina, E., Plant, P. J., Tauxe, C., Thomas, M. A., Münster, C., Chraïbi, A., Pratt, J. H., Horisberger, J., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.7052 · Cited by 711
KOBAYASHI, T., DEAK, M., MORRICE, N., & COHEN, P. (1999) · Biochemical Journal · doi:10.1042/bj3440189 · Cited by 405
Cited by
Matsunaga, K., Saitoh, T., Tabata, K., Omori, H., Satoh, T., Kurotori, N., Maejima, I., Shirahama-Noda, K., Ichimura, T., Isobe, T., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1846 · Cited by 1,235
Self-citationThe Global Phosphorylation Landscape of SARS-CoV-2 Infection
Bouhaddou, M., Memon, D., Meyer, B., White, K. M., Rezelj, V. V., Correa Marrero, M., Polacco, B. J., Melnyk, J. E., Ulferts, S., Kaake, R. M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.034 · Cited by 1,020
García-Martínez, J. M., & Alessi, D. R. (2008) · Biochemical Journal · doi:10.1042/bj20081668 · Cited by 907
(Patho)physiological Significance of the Serum- and Glucocorticoid-Inducible Kinase Isoforms
Lang, F., Böhmer, C., Palmada, M., Seebohm, G., Strutz-Seebohm, N., & Vallon, V. (2006) · Physiological Reviews · doi:10.1152/physrev.00050.2005 · Cited by 689
Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation
Swaney, D. L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N. J., & Villén, J. (2013) · Nature Methods · doi:10.1038/nmeth.2519 · Cited by 599
Metadata
- Authors
- Ichimura, T., Yamamura, H., Sasamoto, K., Tominaga, Y., Taoka, M., Kakiuchi, K., Shinkawa, T., Takahashi, N., Shimada, S., & Isobe, T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-04
- Volume
- 280
- Issue
- 13
- Pages
- 13187-13194
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2119148710
- Cited by
- 193
- References
- 4
- FWCI
- 5.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Ichimura, T., Yamamura, H., Sasamoto, K., Tominaga, Y., Taoka, M., Kakiuchi, K., Shinkawa, T., Takahashi, N., Shimada, S., & Isobe, T. (2005). 14-3-3 Proteins Modulate the Expression of Epithelial Na+ Channels by Phosphorylation-dependent Interaction with Nedd4-2 Ubiquitin Ligase. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m412884200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
