Source:http://linkedlifedata.com/resource/pubmed/id/10747914
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
28
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| pubmed:dateCreated |
2000-8-16
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| pubmed:abstractText |
PRL-1, -2, and -3 represent a novel class of protein-tyrosine phosphatase with a C-terminal prenylation motif. Although PRL-1 has been suggested to be associated with the nucleus, the presence of three highly homologous members and the existence of a prenylation motif call for a more detailed examination of their subcellular localization. In the present study, we first demonstrate that mouse PRL-1, -2, and -3 are indeed prenylated. Examination of N-terminal epitope-tagged PRL-1, -2, and -3 expressed in transiently transfected cells suggests that PRL-1, -2, and -3 are present on the plasma membrane and intracellular punctate structures. Stable Chinese hamster ovary cells expressing PRL-1 and -3 in an inducible manner were established. When cells were treated with brefeldin A, PRL-1 and -3 accumulated in a collapsed compact structure around the microtubule-organizing center. Furthermore, PRL-1 and -3 redistributed into swollen vacuole-like structures when cells were treated with wortmannin. These characteristics of PRL-1 and -3 are typical for endosomal proteins. Electron microscope immunogold labeling reveals that PRL-1 and -3 are indeed associated with the plasma membrane and the early endosomal compartment. Expression of PRL-3 is detected in the epithelial cells of the small intestine, where PRL-3 is present in punctate structures in the cytoplasm. When cells are treated with FTI-277, a selective farnesyltransferase inhibitor, PRL-1, -2, and -3 shifted into the nucleus. Furthermore, a mutant form of PRL-2 lacking the C-terminal prenylation signal is associated with the nucleus. These results establish that the primary association of PRL-1, -2, and -3 with the membrane of the cell surface and the early endosome is dependent on their prenylation and that nuclear localization of these proteins may be triggered by a regulatory event that inhibits their prenylation.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkyl and Aryl Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Brefeldin A,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/FTI 277,
http://linkedlifedata.com/resource/pubmed/chemical/Farnesyltranstransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptp4a1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptp4a2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptp4a3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
14
|
| pubmed:volume |
275
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
21444-52
|
| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10747914-Alkyl and Aryl Transferases,
pubmed-meshheading:10747914-Animals,
pubmed-meshheading:10747914-Brefeldin A,
pubmed-meshheading:10747914-CHO Cells,
pubmed-meshheading:10747914-Cell Membrane,
pubmed-meshheading:10747914-Cricetinae,
pubmed-meshheading:10747914-Endosomes,
pubmed-meshheading:10747914-Enzyme Inhibitors,
pubmed-meshheading:10747914-Farnesyltranstransferase,
pubmed-meshheading:10747914-Immediate-Early Proteins,
pubmed-meshheading:10747914-Intestinal Mucosa,
pubmed-meshheading:10747914-Methionine,
pubmed-meshheading:10747914-Mice,
pubmed-meshheading:10747914-Microvilli,
pubmed-meshheading:10747914-Protein Prenylation,
pubmed-meshheading:10747914-Protein Tyrosine Phosphatases,
pubmed-meshheading:10747914-Recombinant Proteins,
pubmed-meshheading:10747914-Transfection
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| pubmed:year |
2000
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| pubmed:articleTitle |
Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome.
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| pubmed:affiliation |
Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Republic of Singapore.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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