The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Phosphorylation of the PTEN Tail Regulates Protein Stability and Function
Open accessAbstract
The PTEN gene is a tumor suppressor localized in the frequently altered chromosomal region 10q23. The tumor suppressor function of the PTEN protein (PTEN) has been linked to its ability to dephosphorylate the lipid second-messenger phosphatidylinositol 3,4, 5-trisphosphate and phosphatidylinositol 3,4-bisphosphate and, by doing so, to antagonize the phosphoinositide 3-kinase pathway. The PTEN protein consists of an amino-terminal phosphatase domain, a lipid binding C2 domain, and a 50-amino-acid C-terminal domain (the "tail") of unknown function. A number of studies have shown that the tail is dispensable for both phosphatase activity and blocking cell growth. Here, we show that the PTEN tail is necessary for maintaining protein stability and that it also acts to inhibit PTEN function. Thus, removing the tail results in a loss of stability but does not result in a loss of function because the resultant protein is more active. Furthermore, tail-dependent regulation of stability and activity is linked to the phosphorylation of three residues (S380, T382, and T383) within the tail. Therefore, the tail is likely to mediate the regulation of PTEN function through phosphorylation.
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Cites
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The functions and regulation of the PTEN tumour suppressor: new modes and prospects
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Regulation of mammary stem/progenitor cells by PTEN/Akt/β-catenin signaling
Korkaya, H., Paulson, A., Charafe-Jauffret, E., Ginestier, C., Brown, M., Dutcher, J., Clouthier, S. G., & Wicha, M. S. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000121 · Cited by 523
Metadata
- Authors
- Vazquez, F., Ramaswamy, S., Nakamura, N., & Sellers, W. R.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2000-07-01
- Volume
- 20
- Issue
- 14
- Pages
- 5010-5018
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2155737059
- Cited by
- 774
- References
- 47
- FWCI
- 7.66
- Type
- journal article
- Language
- en
- Open access
- green
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- Vazquez, F., Ramaswamy, S., Nakamura, N., & Sellers, W. R. (2000). Phosphorylation of the PTEN Tail Regulates Protein Stability and Function. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.20.14.5010-5018.2000
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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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