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pubmed-article:15899801pubmed:abstractTextAlthough phosphatase and tensin homologue deleted on chromosome 10 (PTEN) localization in the nucleus and cytoplasm is established, the mechanism is unknown. PTEN is a tumor suppressor phosphatase that causes cell cycle arrest and/or apoptosis. Nuclear-cytoplasmic compartmentalization may be a novel mechanism in regulating these events. PTEN does not contain a traditional nuclear localization sequence (NLS); however, we identified putative NLS-like sequences, which we analyzed by site-directed mutagenesis and localization studies in MCF-7 cells. Two double site mutations exhibited nuclear localization defects. Furthermore, unlike wild-type PTEN, double NLS mutant PTEN did not interact with major vault protein (MVP), a previously hypothesized nuclear-cytoplasmic transport protein. We conclude that these two NLS-like sequences are required for PTEN nuclear import that is mediated by MVP. Further, we show that this MVP-mediated nuclear import is independent of PTEN phosphorylation and of the lipid and protein phosphatase activities of PTEN.lld:pubmed
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pubmed-article:15899801pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:15899801pubmed:articleTitlePhosphatase and tensin homologue deleted on chromosome 10 (PTEN) has nuclear localization signal-like sequences for nuclear import mediated by major vault protein.lld:pubmed
pubmed-article:15899801pubmed:affiliationClinical Cancer Genetics Program, Human Cancer Genetics Program, Comprehensive Cancer Center, Columbus, Ohio 43210, USA.lld:pubmed
pubmed-article:15899801pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15899801pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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pubmed-article:15899801pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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