Journal
NATURE CELL BIOLOGY
Volume 13, Issue 6, Pages 728-U224Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb2240
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Funding
- Ministry of Science and Technology, India [BT/PR13134/GBD/27/202/2009]
- Era of Hope Research Scholar Award [W81XWH-09-0409]
- NIH [CA108961]
- Department of Defense [W81XWH-05-0470]
- Council of Scientific and Industrial Research
- University Grants Commission, India
- Department of Biotechnology
- Institute of Life Sciences, Hyderabad
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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-l-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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