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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2001-2-22
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pubmed:databankReference |
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pubmed:abstractText |
Members of the AF4/FMR2 family of nuclear proteins are involved in human diseases such as acute lymphoblastic leukemia and mental retardation. Here we report the identification and characterization of the Drosophila lilliputian (lilli) gene, which encodes a nuclear protein related to mammalian AF4 and FMR2. Mutations in lilli suppress excessive neuronal differentiation in response to a constitutively active form of Raf in the eye. In the wild type, Lilli has a partially redundant function in the Ras/MAPK pathway in differentiation but it is essential for normal growth. Loss of Lilli function causes an autonomous reduction in cell size and partially suppresses the increased growth associated with loss of PTEN function. These results suggest that Lilli acts in parallel with the Ras/MAPK and the PI3K/PKB pathways in the control of cell identity and cellular growth.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTEN Phosphohydrolase,
http://linkedlifedata.com/resource/pubmed/chemical/PTEN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0950-1991
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
128
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
791-800
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11171403-Amino Acid Sequence,
pubmed-meshheading:11171403-Animals,
pubmed-meshheading:11171403-Animals, Genetically Modified,
pubmed-meshheading:11171403-Cell Differentiation,
pubmed-meshheading:11171403-Cell Nucleus,
pubmed-meshheading:11171403-Cell Size,
pubmed-meshheading:11171403-DNA,
pubmed-meshheading:11171403-Drosophila Proteins,
pubmed-meshheading:11171403-Drosophila melanogaster,
pubmed-meshheading:11171403-Embryo, Nonmammalian,
pubmed-meshheading:11171403-Embryonic Development,
pubmed-meshheading:11171403-Genes, Insect,
pubmed-meshheading:11171403-Germ-Line Mutation,
pubmed-meshheading:11171403-Humans,
pubmed-meshheading:11171403-Insect Proteins,
pubmed-meshheading:11171403-MAP Kinase Signaling System,
pubmed-meshheading:11171403-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11171403-Molecular Sequence Data,
pubmed-meshheading:11171403-Nuclear Proteins,
pubmed-meshheading:11171403-PTEN Phosphohydrolase,
pubmed-meshheading:11171403-Phenotype,
pubmed-meshheading:11171403-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:11171403-Phosphoric Monoester Hydrolases,
pubmed-meshheading:11171403-Photoreceptor Cells, Invertebrate,
pubmed-meshheading:11171403-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11171403-Proto-Oncogene Proteins,
pubmed-meshheading:11171403-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:11171403-Sequence Alignment,
pubmed-meshheading:11171403-Signal Transduction,
pubmed-meshheading:11171403-Transcription Factors,
pubmed-meshheading:11171403-Tumor Suppressor Proteins,
pubmed-meshheading:11171403-ras Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Lilliputian: an AF4/FMR2-related protein that controls cell identity and cell growth.
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pubmed:affiliation |
Zoologisches Institut, Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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