rdf:type |
|
lifeskim:mentions |
umls-concept:C0023689,
umls-concept:C0041538,
umls-concept:C0851285,
umls-concept:C1120843,
umls-concept:C1366876,
umls-concept:C1514873,
umls-concept:C1527148,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1704259,
umls-concept:C1705987
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pubmed:issue |
3
|
pubmed:dateCreated |
2005-2-14
|
pubmed:abstractText |
Synapses display a stereotyped ultrastructural organization, commonly containing a single electron-dense presynaptic density surrounded by a cluster of synaptic vesicles. The mechanism controlling subsynaptic proportion is not understood. Loss of function in the C. elegans rpm-1 gene, a putative RING finger/E3 ubiquitin ligase, causes disorganized presynaptic cytoarchitecture. RPM-1 is localized to the presynaptic periactive zone. We report that RPM-1 negatively regulates a p38 MAP kinase pathway composed of the dual leucine zipper-bearing MAPKKK DLK-1, the MAPKK MKK-4, and the p38 MAP kinase PMK-3. Inactivation of this pathway suppresses rpm-1 loss of function phenotypes, whereas overexpression or constitutive activation of this pathway causes synaptic defects resembling rpm-1(lf) mutants. DLK-1, like RPM-1, is localized to the periactive zone. DLK-1 protein levels are elevated in rpm-1 mutants. The RPM-1 RING finger can stimulate ubiquitination of DLK-1. Our data reveal a presynaptic role of a previously unknown p38 MAP kinase cascade.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RPM-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/mitogen-activated protein kinase...,
http://linkedlifedata.com/resource/pubmed/chemical/p38 Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/pmk-3 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
|
pubmed:issn |
0092-8674
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
11
|
pubmed:volume |
120
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
407-20
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:15707898-Animals,
pubmed-meshheading:15707898-Caenorhabditis elegans,
pubmed-meshheading:15707898-Caenorhabditis elegans Proteins,
pubmed-meshheading:15707898-Cell Differentiation,
pubmed-meshheading:15707898-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:15707898-MAP Kinase Kinase Kinases,
pubmed-meshheading:15707898-MAP Kinase Signaling System,
pubmed-meshheading:15707898-Microscopy, Electron, Transmission,
pubmed-meshheading:15707898-Mitogen-Activated Protein Kinases,
pubmed-meshheading:15707898-Mutation,
pubmed-meshheading:15707898-Nervous System,
pubmed-meshheading:15707898-Presynaptic Terminals,
pubmed-meshheading:15707898-Protein Structure, Tertiary,
pubmed-meshheading:15707898-Ubiquitin,
pubmed-meshheading:15707898-p38 Mitogen-Activated Protein Kinases
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pubmed:year |
2005
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pubmed:articleTitle |
Regulation of a DLK-1 and p38 MAP kinase pathway by the ubiquitin ligase RPM-1 is required for presynaptic development.
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pubmed:affiliation |
Department of Molecular, Cell, and Developmental Biology, University of California, Santa Cruz, Santa Cruz, California 95064, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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