Article: article from journal or magazin.
Drosophila 14-3-3/PAR-5 is an essential mediator of PAR-1 function in axis formation.
Publication types: Journal Article ; Research Support, Non-U.S. Gov't Publication Status: ppublish
PAR-1 kinases are required to determine the anterior-posterior (A-P) axis in C. elegans and Drosophila, but little is known about their molecular function. We identified 14-3-3 proteins as Drosophila PAR-1 interactors and show that PAR-1 binds a domain of 14-3-3 distinct from the phosphoserine binding pocket. PAR-1 kinases phosphorylate proteins to generate 14-3-3 binding sites and may therefore directly deliver 14-3-3 to these targets. 14-3-3 mutants display identical phenotypes to par-1 mutants in oocyte determination and the polarization of the A-P axis. Together, these results indicate that PAR-1's function is mediated by the binding of 14-3-3 to its substrates. The C. elegans 14-3-3 protein, PAR-5, is also required for A-P polarization, suggesting that this is a conserved mechanism by which PAR-1 establishes cellular asymmetries.
14-3-3 Proteins, Animals, Axis/physiology, Binding Sites, Caenorhabditis elegans Proteins, Cell Polarity, Drosophila Proteins/genetics, Drosophila Proteins/metabolism, Drosophila melanogaster/genetics, Drosophila melanogaster/metabolism, Female, Germ Cells, Oocytes/metabolism, Phosphorylation, Protein-Serine-Threonine Kinases/genetics, Protein-Serine-Threonine Kinases/metabolism, Tyrosine 3-Monooxygenase/chemistry, Tyrosine 3-Monooxygenase/genetics
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