The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
WWP2 is an E3 ubiquitin ligase for PTEN
Open accessAbstract
PTEN, a lipid phosphatase, is one of the most frequently mutated tumour suppressors in human cancer. Several recent studies have highlighted the importance of ubiquitylation in regulating PTEN tumour-suppressor function, but the enzymatic machinery required for PTEN ubiquitylation is not clear. In this study, by using a tandem affinity-purification approach, we have identified WWP2 (also known as atrophin-1-interacting protein 2, AIP-2) as a PTEN-interacting protein. WWP2 is an E3 ubiquitin ligase that belongs to the NEDD4-like protein family, which is involved in regulating transcription, embryonic stem-cell fate, cellular transport and T-cell activation processes. We show that WWP2 physically interacts with PTEN and mediates its degradation through a ubiquitylation-dependent pathway. Functionally, we show that WWP2 controls cellular apoptosis and is required for tumorigenicity of cells. Collectively, our results reveal a functional E3 ubiquitin ligase for PTEN that plays a vital role in tumour-cell survival.
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Pten is essential for embryonic development and tumour suppression
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The lipid phosphatase activity of PTEN is critical for its tumor supressor function
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Regulation of PTEN Transcription by p53
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Cited by
The functions and regulation of the PTEN tumour suppressor
Song, M. S., Salmena, L., & Pandolfi, P. P. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3330 · Cited by 1,926
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638
Microenvironment-induced PTEN loss by exosomal microRNA primes brain metastasis outgrowth
Zhang, L., Zhang, S., Yao, J., Lowery, F. J., Zhang, Q., Huang, W.-C., Li, P., Li, M., Wang, X., Zhang, C., et al. (2015) · Nature · doi:10.1038/nature15376 · Cited by 1,175
The functions and regulation of the PTEN tumour suppressor: new modes and prospects
Lee, Y.-R., Chen, M., & Pandolfi, P. P. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0015-0 · Cited by 917
The role of ubiquitination in tumorigenesis and targeted drug discovery
Deng, L., Meng, T., Chen, L., Wei, W., & Wang, P. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0107-0 · Cited by 744
Metadata
- Authors
- Maddika, S., Kavela, S., Rani, N., Palicharla, V. R., Pokorny, J. L., Sarkaria, J. N., & Chen, J.
- Venue
- Nature Cell Biology
- Published
- 2011-05-01
- Volume
- 13
- Issue
- 6
- Pages
- 728-733
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2067576594
- Cited by
- 305
- References
- 41
- FWCI
- 7.88
- Type
- journal article
- Language
- en
- Open access
- green
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- Maddika, S., Kavela, S., Rani, N., Palicharla, V. R., Pokorny, J. L., Sarkaria, J. N., & Chen, J. (2011). WWP2 is an E3 ubiquitin ligase for PTEN. Nature Cell Biology. https://doi.org/10.1038/ncb2240
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