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Título: | A functional dissection of PTEN N-terminus: Implications in PTEN subcellular targeting and tumor suppressor activity |
Autor: | Gil, Anabel CSIC; Rodríguez-Escudero, Isabel; Stumpf, Miriam; Molina, María; Cid, Víctor J.; Pulido, Rafael | Fecha de publicación: | 15-abr-2015 | Editor: | Public Library of Science | Citación: | PLoS ONE 10(4): e0119287 (2015) | Resumen: | Spatial regulation of the tumor suppressor PTEN is exerted through alternative plasma membrane, cytoplasmic, and nuclear subcellular locations. The N-terminal region of PTEN is important for the control of PTEN subcellular localization and function. It contains both an active nuclear localization signal (NLS) and an overlapping PIP2-binding motif (PBM) involved in plasma membrane targeting. We report a comprehensive mutational and functional analysis of the PTEN N-terminus, including a panel of tumor-related mutations at this region. Nuclear/cytoplasmic partitioning in mammalian cells and PIP3 phosphatase assays in reconstituted S. cerevisiae defined categories of PTEN N-terminal mutations with distinct PIP3 phosphatase and nuclear accumulation properties. Noticeably, most tumor-related mutations that lost PIP3 phosphatase activity also displayed impaired nuclear localization. Cell proliferation and soft-agar colony formation analysis in mammalian cells of mutations with distinctive nuclear accumulation and catalytic activity patterns suggested a contribution of both properties to PTEN tumor suppressor activity. Our functional dissection of the PTEN N-terminus provides the basis for a systematic analysis of tumor-related and experimentally engineered PTEN mutations. | Descripción: | © 2015 Gil et al. | Versión del editor: | http://dx.doi.org/10.1371/journal.pone.0119287 | URI: | http://hdl.handle.net/10261/199323 | DOI: | 10.1371/journal.pone.0119287 | E-ISSN: | 1932-6203 |
Aparece en las colecciones: | (IC) Artículos |
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