Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2004-11-12
pubmed:abstractText
The Ser/Thr kinase Par-1 is required for cell polarisation in diverse organisms such as yeast, worms, flies and mammals. During Drosophila oogenesis, Par-1 is required for several polarisation events, including localisation of the anterior determinant bicoid. To elucidate the molecular pathways triggered by Par-1, we have performed a genome-wide, high-throughput screen for Par-1 targets. Among the targets identified in this screen was Exuperantia (Exu), a mediator of bicoid mRNA localisation. We show that Exu is a phosphoprotein whose phosphorylation is dependent on Par-1 in vitro and in vivo. We identify two motifs in Exu that are phosphorylated by Par-1, and show that their mutation abolishes bicoid mRNA localisation during mid-oogenesis. Interestingly, exu mutants in which Exu phosphorylation is specifically affected can to some extent recover from these bicoid mRNA localisation defects during late oogenesis. These results demonstrate that Par-1 establishes polarity in the oocyte by activating a mediator of bicoid mRNA localisation. Furthermore, our analysis reveals two phases of Exu-dependent bicoid mRNA localisation: an early phase that is strictly dependent on Exu phosphorylation and a late phase that is less phosphorylation dependent.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Egg Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Par-1 protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/bicoid protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/exu protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0950-1991
pubmed:author
pubmed:issnType
Print
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5897-907
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15539486-Amino Acid Motifs, pubmed-meshheading:15539486-Animals, pubmed-meshheading:15539486-Blotting, Western, pubmed-meshheading:15539486-Drosophila Proteins, pubmed-meshheading:15539486-Drosophila melanogaster, pubmed-meshheading:15539486-Egg Proteins, pubmed-meshheading:15539486-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15539486-Embryo, Nonmammalian, pubmed-meshheading:15539486-Expressed Sequence Tags, pubmed-meshheading:15539486-Female, pubmed-meshheading:15539486-Gene Expression Regulation, Developmental, pubmed-meshheading:15539486-Homeodomain Proteins, pubmed-meshheading:15539486-In Situ Hybridization, pubmed-meshheading:15539486-Microscopy, Fluorescence, pubmed-meshheading:15539486-Models, Genetic, pubmed-meshheading:15539486-Mutagenesis, pubmed-meshheading:15539486-Mutation, pubmed-meshheading:15539486-Ovary, pubmed-meshheading:15539486-Phosphorylation, pubmed-meshheading:15539486-Protein Kinases, pubmed-meshheading:15539486-Protein-Serine-Threonine Kinases, pubmed-meshheading:15539486-RNA, Messenger, pubmed-meshheading:15539486-RNA-Binding Proteins, pubmed-meshheading:15539486-Trans-Activators, pubmed-meshheading:15539486-Transgenes
pubmed:year
2004
pubmed:articleTitle
Par-1 regulates bicoid mRNA localisation by phosphorylating Exuperantia.
pubmed:affiliation
European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't