rdf:type |
|
lifeskim:mentions |
umls-concept:C0008652,
umls-concept:C0031678,
umls-concept:C0127400,
umls-concept:C0162326,
umls-concept:C0168424,
umls-concept:C0293442,
umls-concept:C0475264,
umls-concept:C0521447,
umls-concept:C0694888,
umls-concept:C0887839,
umls-concept:C1334043,
umls-concept:C1553877,
umls-concept:C1608885,
umls-concept:C1880274
|
pubmed:issue |
10
|
pubmed:dateCreated |
2005-5-18
|
pubmed:abstractText |
Although 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.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0008-5472
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
65
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4108-16
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:15899801-Breast Neoplasms,
pubmed-meshheading:15899801-Cell Line, Tumor,
pubmed-meshheading:15899801-Cell Nucleus,
pubmed-meshheading:15899801-Cytoplasm,
pubmed-meshheading:15899801-Humans,
pubmed-meshheading:15899801-Karyopherins,
pubmed-meshheading:15899801-Mutagenesis, Site-Directed,
pubmed-meshheading:15899801-Mutation,
pubmed-meshheading:15899801-Nuclear Localization Signals,
pubmed-meshheading:15899801-PTEN Phosphohydrolase,
pubmed-meshheading:15899801-Phosphoric Monoester Hydrolases,
pubmed-meshheading:15899801-Phosphorylation,
pubmed-meshheading:15899801-Structure-Activity Relationship,
pubmed-meshheading:15899801-Transfection,
pubmed-meshheading:15899801-Tumor Suppressor Proteins,
pubmed-meshheading:15899801-Vault Ribonucleoprotein Particles
|
pubmed:year |
2005
|
pubmed:articleTitle |
Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) has nuclear localization signal-like sequences for nuclear import mediated by major vault protein.
|
pubmed:affiliation |
Clinical Cancer Genetics Program, Human Cancer Genetics Program, Comprehensive Cancer Center, Columbus, Ohio 43210, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|