Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2004-5-11
pubmed:abstractText
Drosophila PTEN (dPTEN) plays indispensable roles in the development of Drosophila melanogaster by controlling cell size and number. Although three potential spliced forms of dPTEN have been isolated, functional distinction among these forms remains elusive. In this study, we demonstrate that all spliced forms of dPTEN dephosphorylate phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P(3)); however, PI(3,4,5)P(3)-dependent activation of Drosophila Akt is suppressed specifically by one of three spliced forms, dPTEN3. Further, dPTEN3 dramatically changes its expression during the Drosophila development, while the other forms are expressed throughout the development. Our results suggest that dPTEN3 is the predominant spliced form that participates in PI(3,4,5)P(3)-mediated signaling pathways.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase, http://linkedlifedata.com/resource/pubmed/chemical/PTEN Phosphohydrolase, http://linkedlifedata.com/resource/pubmed/chemical/PTEN protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylinositol...
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
565
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:15135050-Alternative Splicing, pubmed-meshheading:15135050-Animals, pubmed-meshheading:15135050-Cell Line, pubmed-meshheading:15135050-DNA, Complementary, pubmed-meshheading:15135050-Drosophila Proteins, pubmed-meshheading:15135050-Drosophila melanogaster, pubmed-meshheading:15135050-Glutathione Transferase, pubmed-meshheading:15135050-Microscopy, Confocal, pubmed-meshheading:15135050-Mutation, pubmed-meshheading:15135050-PTEN Phosphohydrolase, pubmed-meshheading:15135050-Phosphatidylinositol 3-Kinases, pubmed-meshheading:15135050-Phosphatidylinositol Phosphates, pubmed-meshheading:15135050-Phosphoric Monoester Hydrolases, pubmed-meshheading:15135050-Phosphorylation, pubmed-meshheading:15135050-Plasmids, pubmed-meshheading:15135050-RNA, Messenger, pubmed-meshheading:15135050-Recombinant Proteins, pubmed-meshheading:15135050-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:15135050-Signal Transduction, pubmed-meshheading:15135050-Time Factors, pubmed-meshheading:15135050-Transfection
pubmed:year
2004
pubmed:articleTitle
Suppression of a phosphatidylinositol 3-kinase signal by a specific spliced variant of Drosophila PTEN.
pubmed:affiliation
Department of Pharmacology, Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Tokyo 113-8613, Japan. tmaehama@rinshoken.or.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't