Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M111.221184
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dc.titleProtein interactions of phosphatase and tensin homologue (PTEN) and its cancer-associated G20E mutant compared by using stable isotope labeling by amino acids in cell culture-based parallel affinity purification
dc.contributor.authorGunaratne, J.
dc.contributor.authorGoh, M.X.
dc.contributor.authorSwa, H.L.F.
dc.contributor.authorLee, F.Y.
dc.contributor.authorEMMA MAY SANFORD
dc.contributor.authorWong, L.M.
dc.contributor.authorHogue, K.A.
dc.contributor.authorBlackstock, W.P.
dc.contributor.authorOkumura, K.
dc.date.accessioned2014-12-12T07:51:09Z
dc.date.available2014-12-12T07:51:09Z
dc.date.issued2011-05-20
dc.identifier.citationGunaratne, J., Goh, M.X., Swa, H.L.F., Lee, F.Y., EMMA MAY SANFORD, Wong, L.M., Hogue, K.A., Blackstock, W.P., Okumura, K. (2011-05-20). Protein interactions of phosphatase and tensin homologue (PTEN) and its cancer-associated G20E mutant compared by using stable isotope labeling by amino acids in cell culture-based parallel affinity purification. Journal of Biological Chemistry 286 (20) : 18093-18103. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M111.221184
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/116542
dc.description.abstractThe tumor suppressor PTEN (phosphatase and tensin homologue) negatively regulates the PI3K pathway through its lipid phosphatase activity and is one of the most commonly lost tumor suppressors in human cancers. Though the tumor suppressive function involves the lipid phosphatase-dependent and -independent activities of PTEN, the mechanism leading to the phosphatase-independent function of PTEN is understood poorly. Some PTEN mutants have lipid phosphatase activity but fail to suppress cell growth. Here, we use a cancer-associated mutant, G20E, to gain insight into the phosphatase-independent function of PTEN by investigating protein-protein interactions using MS-based stable isotope labeling by amino acids in cell culture (SILAC). A strategy named parallel affinity purification (PAP) and SILAC has been developed to prioritize interactors and to compare the interactions between wild-type and G20E PTEN. Clustering of the prioritized interactors acquired by the PAP-SILAC approach shows three distinct clusters: 1) wild-type-specific interactors, 2) interactors unique to the G20E mutant, and 3) proteins common to wild-type and mutant. These interactors are involved mainly in cell migration and apoptosis pathways. We further demonstrate that the wild-typespecific interactor, NUDTL16L1, is required for the regulatory function of wild-type PTEN in cell migration. These findings contribute to a better understanding of the mechanisms of the phosphatase-dependent and -independent functions of PTEN. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.M111.221184
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCANCER SCIENCE INSTITUTE OF SINGAPORE
dc.description.doi10.1074/jbc.M111.221184
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume286
dc.description.issue20
dc.description.page18093-18103
dc.description.codenJBCHA
dc.identifier.isiut000290585200070
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