Abstract
Par-1 kinase is critical for polarization of the Drosophila melanogaster oocyte and the one-cell Caenorhabditis elegans embryo. Although Par-1 localizes specifically to the posterior pole in both cells, neither its targets nor its function at the posterior pole have been elucidated. Here we show that Drosophila Par-1 phosphorylates the posterior determinant Oskar (Osk) and demonstrate genetically that Par-1 is required for accumulation of Osk protein. We show in cell-free extracts that Osk protein is intrinsically unstable and that it is stabilized after phosphorylation by Par-1. Our data indicate that posteriorly localized Par-1 regulates posterior patterning by stabilizing Osk.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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3' Untranslated Regions / metabolism
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Animals
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Body Patterning*
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Caenorhabditis elegans / embryology
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Caenorhabditis elegans / metabolism
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Caenorhabditis elegans Proteins*
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Cysteine Endopeptidases / metabolism
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Drosophila Proteins / genetics
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Drosophila Proteins / metabolism*
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Drosophila melanogaster / embryology
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Drosophila melanogaster / metabolism
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Embryo, Nonmammalian / anatomy & histology
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Embryo, Nonmammalian / physiology*
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Female
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Models, Biological
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Multienzyme Complexes / metabolism
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Ovary / chemistry
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Ovary / metabolism
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Phosphorylation
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Proteasome Endopeptidase Complex
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism*
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Recombinant Fusion Proteins / metabolism
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Tissue Extracts / chemistry
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Tissue Extracts / metabolism
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Ubiquitin / metabolism
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Xenopus laevis / metabolism
Substances
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3' Untranslated Regions
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Caenorhabditis elegans Proteins
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Drosophila Proteins
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Multienzyme Complexes
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Recombinant Fusion Proteins
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Tissue Extracts
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Ubiquitin
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osk protein, Drosophila
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PAR-1 protein, C elegans
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Protein Serine-Threonine Kinases
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex