Source:http://linkedlifedata.com/resource/pubmed/id/16378591
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2006-1-3
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pubmed:abstractText |
Mammalian WASP and N-WASP are involved in reorganization of the actin cytoskeleton through activation of the Arp2/3 complex and in regulation of cell motility or cell shape changes. In the present study, we identified WASP-interacting protein homologue (WIP)-1 in Caenorhabditis elegans. WIP-1 contains the domains and sequences conserved among mammalian WIP family proteins. Yeast two-hybrid analysis detected a physical interaction between WIP-1 and WSP-1, the sole homologue of WASP/N-WASP in C. elegans. Western analysis of embryo lysates showed that RNA interference (RNAi) treatment for wip-1 decreased levels of WSP-1 protein, and wsp-1(RNAi) treatment decreased levels of WIP-1 protein. However, wsp-1 mRNA levels were not decreased in wip-1(RNAi)-treated embryos, and wip-1 mRNA levels were not decreased in wsp-1(RNAi)-treated embryos. Furthermore, disruption of WIP-1 by RNAi resulted in embryonic lethality with morphologic defects in hypodermal cell migration, a process known as ventral enclosure. This phenotype was similar to that observed in RNAi experiments for wsp-1. Immunostaining showed that WIP-1 was expressed by migrating hypodermal cells, as was WSP-1. This expression during ventral enclosure was reduced in wip-1(RNAi)-treated embryos and wsp-1(RNAi)-treated embryos. Our results suggest that C. elegans WIP-1 may function in hypodermal cell migration during ventral enclosure by maintaining levels of WSP-1.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Wiskott-Aldrich Syndrome Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase 2C
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
340
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
709-17
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16378591-Amino Acid Sequence,
pubmed-meshheading:16378591-Animals,
pubmed-meshheading:16378591-Caenorhabditis elegans,
pubmed-meshheading:16378591-Caenorhabditis elegans Proteins,
pubmed-meshheading:16378591-Carrier Proteins,
pubmed-meshheading:16378591-Cell Movement,
pubmed-meshheading:16378591-Cloning, Molecular,
pubmed-meshheading:16378591-Molecular Sequence Data,
pubmed-meshheading:16378591-Morphogenesis,
pubmed-meshheading:16378591-Neoplasm Proteins,
pubmed-meshheading:16378591-Phosphoprotein Phosphatases,
pubmed-meshheading:16378591-RNA Interference,
pubmed-meshheading:16378591-Subcutaneous Tissue,
pubmed-meshheading:16378591-Wiskott-Aldrich Syndrome Protein Family
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pubmed:year |
2006
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pubmed:articleTitle |
Caenorhabditis elegans WASP-interacting protein homologue WIP-1 is involved in morphogenesis through maintenance of WSP-1 protein levels.
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pubmed:affiliation |
Department of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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