Abstract
We show that loss-of-function mutations in kinases of the MLK-1 pathway (mlk-1, mek-1, and kgb-1/jnk) function cell-autonomously in neurons to suppress defects in synapse formation and axon termination caused by rpm-1 loss of function. Our genetic analysis also suggests that the phosphatase PPM-1, like RPM-1, is a potential inhibitor of kinases in the MLK-1 pathway.
Keywords:
JNK; MAP kinase; RPM-1; axon; synapse.
Copyright © 2015 by the Genetics Society of America.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Axons / metabolism
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Caenorhabditis elegans / genetics*
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Caenorhabditis elegans / growth & development
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Caenorhabditis elegans Proteins / genetics*
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Caenorhabditis elegans Proteins / metabolism
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Guanine Nucleotide Exchange Factors / genetics
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Guanine Nucleotide Exchange Factors / metabolism
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JNK Mitogen-Activated Protein Kinases / genetics*
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JNK Mitogen-Activated Protein Kinases / metabolism
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MAP Kinase Kinase 1 / genetics*
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MAP Kinase Kinase 1 / metabolism
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MAP Kinase Signaling System*
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Neurogenesis*
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Synapses / metabolism
Substances
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Caenorhabditis elegans Proteins
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Guanine Nucleotide Exchange Factors
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RPM-1 protein, C elegans
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JNK Mitogen-Activated Protein Kinases
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KGB-1 protein, C elegans
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MAP Kinase Kinase 1