Abstract
In C. elegans, the anchor cell signal induces Pn.p cells to form the vulva by activating a conserved receptor tyrosine kinase pathway. lin-2 and lin-7 mutants exhibit a vulvaless phenotype similar to the phenotype observed when this signaling pathway is defective. We have found that LIN-7 is a cell junction-associated protein that binds to the LET-23 receptor tyrosine kinase. LET-23 is also localized to the cell junctions, and both LIN-2 and LIN-7 are required for this localization. LET-23 overexpression rescues the lin-2 or lin-7 vulvaless phenotype, suggesting that increased receptor density can compensate for mislocalization. These results suggest that proper localization of LET-23 receptor to the Pn.p cell junctions is required for signaling activity.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Base Sequence
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Caenorhabditis elegans / genetics*
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Caenorhabditis elegans Proteins*
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Cloning, Molecular
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Embryonic Induction / genetics
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Epithelium / chemistry
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Epithelium / physiology
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Epithelium / ultrastructure
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ErbB Receptors / genetics*
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Female
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Genes, Helminth / physiology
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Helminth Proteins / genetics*
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Helminth Proteins / physiology
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Intercellular Junctions / chemistry*
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Membrane Proteins / genetics*
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Membrane Proteins / physiology
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Molecular Sequence Data
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Mutation / physiology
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Phenotype
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Protein Structure, Tertiary
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Proteins*
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Sequence Homology, Amino Acid
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Signal Transduction / genetics
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Vulva / cytology
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Vulva / growth & development
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Vulva / physiology
Substances
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Caenorhabditis elegans Proteins
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Helminth Proteins
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LIN-7 protein, C elegans
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Lin-2 protein, C elegans
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Membrane Proteins
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Proteins
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lin-10 protein, C elegans
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ErbB Receptors
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let-23 protein, C elegans