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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2009-4-9
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pubmed:abstractText |
The nematode cuticle is a tough extracellular matrix composed primarily of cross-linked collagens and non-collagenous cuticulins. It is required for nematode motility and protection from the external environment. Little is known about how the complex process of cuticle formation has been adapted to the specialized requirements of the nematode cuticle, which is structurally and compositionally unique from other organisms. The C. elegans gene cuti-1 (CUTicle and epithelial Integrity) encodes a nematode-specific protein. We have shown that CUTI-1 is expressed in the epithelia and in seam cells. Within these tissues the expression of cuti-1 mRNA cycles throughout development in line with the molting cycle, a process that involves synthesis of a new cuticle. In addition, knockdown of cuti-1 by RNA interference (RNAi) results in worms that display post-embryonic phenotypes related to cuticle dysfunction and defects in epithelial integrity. This is one of the first reports of a nematode-specific protein involved in extracellular matrix formation. It provides further insight into how novel ways have evolved to regulate the formation of the cuticle, which is the primary protective barrier and skeletal component of nematodes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19357781-10444073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19357781-10637627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19357781-10996790,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19357781-15837622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19357781-1860880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19357781-2586513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19357781-4366476,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19357781-9486653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19357781-9804418
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e5117
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:19357781-Amino Acid Sequence,
pubmed-meshheading:19357781-Animals,
pubmed-meshheading:19357781-Caenorhabditis elegans,
pubmed-meshheading:19357781-Caenorhabditis elegans Proteins,
pubmed-meshheading:19357781-Epithelium,
pubmed-meshheading:19357781-Extracellular Matrix,
pubmed-meshheading:19357781-Genes, Reporter,
pubmed-meshheading:19357781-Membrane Proteins,
pubmed-meshheading:19357781-Molecular Sequence Data,
pubmed-meshheading:19357781-RNA Interference,
pubmed-meshheading:19357781-Recombinant Fusion Proteins,
pubmed-meshheading:19357781-Sequence Alignment,
pubmed-meshheading:19357781-Sequence Homology, Amino Acid,
pubmed-meshheading:19357781-Two-Hybrid System Techniques,
pubmed-meshheading:19357781-Vesicular Transport Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
CUTI-1: A novel tetraspan protein involved in C. elegans CUTicle formation and epithelial integrity.
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pubmed:affiliation |
Biochemistry & Molecular Biology, The School of Biology, College of Medicine, Biology and Environment, The Australian National University, Canberra, Australian Capital Territory, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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