Source:http://linkedlifedata.com/resource/pubmed/id/20881202
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
2010-12-16
|
pubmed:abstractText |
DEG/ENaC channels have been broadly implicated in mechanosensory transduction, yet many questions remain about how these proteins contribute to complexes that sense mechanical stimuli. In C. elegans, two DEG/ENaC channel subunits are thought to contribute to a gentle touch transduction complex: MEC-4, which is essential for gentle touch sensation, and MEC-10, whose importance is less well defined. By characterizing a mec-10 deletion mutant, we have found that MEC-10 is important, but not essential, for gentle touch responses in the body touch neurons ALM, PLM, and PVM. Surprisingly, the requirement for MEC-10 in ALM and PLM is spatially asymmetric; mec-10 animals show significant behavioral and physiological responses to stimulation at the distal end of touch neuron dendrites, but respond poorly to stimuli applied near the neuronal cell body. The subcellular distribution of a rescuing MEC-10::GFP translational fusion was found to be restricted to the neuronal cell body and proximal dendrite, consistent with the hypothesis that MEC-10 protein is asymmetrically distributed within the touch neuron process. These results suggest that MEC-10 may contribute to only a subset of gentle touch mechanosensory complexes found preferentially at the proximal dendrite.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MEC-10 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Mec-4 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
1522-1598
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:volume |
104
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3334-44
|
pubmed:meshHeading |
pubmed-meshheading:20881202-Alleles,
pubmed-meshheading:20881202-Animals,
pubmed-meshheading:20881202-Animals, Genetically Modified,
pubmed-meshheading:20881202-Caenorhabditis elegans,
pubmed-meshheading:20881202-Caenorhabditis elegans Proteins,
pubmed-meshheading:20881202-Calcium,
pubmed-meshheading:20881202-Dendrites,
pubmed-meshheading:20881202-Gene Deletion,
pubmed-meshheading:20881202-Green Fluorescent Proteins,
pubmed-meshheading:20881202-Mechanotransduction, Cellular,
pubmed-meshheading:20881202-Membrane Proteins,
pubmed-meshheading:20881202-Recombinant Fusion Proteins,
pubmed-meshheading:20881202-Sensory Receptor Cells,
pubmed-meshheading:20881202-Subcellular Fractions,
pubmed-meshheading:20881202-Touch
|
pubmed:year |
2010
|
pubmed:articleTitle |
Spatial asymmetry in the mechanosensory phenotypes of the C. elegans DEG/ENaC gene mec-10.
|
pubmed:affiliation |
Cell Biology Division, MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
|
pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|