rdf:type |
|
lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0043342,
umls-concept:C0086376,
umls-concept:C0376449,
umls-concept:C1171362,
umls-concept:C1425441,
umls-concept:C1514873,
umls-concept:C1515670,
umls-concept:C1519227,
umls-concept:C1522492,
umls-concept:C1538857,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C2587213
|
pubmed:issue |
11
|
pubmed:dateCreated |
2009-10-28
|
pubmed:abstractText |
The process of segmentation in vertebrates is described by a clock and wavefront model consisting of a Notch signal and an fibroblast growth factor-8 (FGF8) gradient, respectively. To further investigate the segmentation process, we screened gene expression profiles for downstream targets of the segmentation clock. The Rnd1 and Rnd3 GTP-binding proteins comprise a subgroup of the Rho GTPase family that show a specific expression pattern similar to the Notch signal component ESR5, suggesting an association between Rnd1/3 and the segmentation clock. Rnd1/3 expression patterns are disrupted by overexpression of dominant-negative or active forms of Notch signaling genes, and responds to the FGF inhibitor SU5402 by a posterior shift analogous to other segmentation-related genes, suggesting that Rnd1/3 expressions are regulated by the segmentation clock machinery. We also show that antisense morpholino oligonucleotides to Rnd1/3 inhibit somite segmentation and differentiation in Xenopus embryos. These results suggest that Rnd1/3 are required for Xenopus somitogenesis.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factors,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrroles,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Notch,
http://linkedlifedata.com/resource/pubmed/chemical/SU 5402,
http://linkedlifedata.com/resource/pubmed/chemical/XRnd1 protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
|
pubmed:issn |
1097-0177
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pubmed:author |
|
pubmed:copyrightInfo |
Copyright 2009 Wiley-Liss, Inc.
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pubmed:issnType |
Electronic
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pubmed:volume |
238
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2867-76
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pubmed:meshHeading |
pubmed-meshheading:19795516-Animals,
pubmed-meshheading:19795516-Cell Differentiation,
pubmed-meshheading:19795516-Embryo, Nonmammalian,
pubmed-meshheading:19795516-Fibroblast Growth Factors,
pubmed-meshheading:19795516-GTP-Binding Proteins,
pubmed-meshheading:19795516-Oligonucleotides, Antisense,
pubmed-meshheading:19795516-Pyrroles,
pubmed-meshheading:19795516-Receptors, Notch,
pubmed-meshheading:19795516-Somites,
pubmed-meshheading:19795516-Xenopus Proteins,
pubmed-meshheading:19795516-Xenopus laevis,
pubmed-meshheading:19795516-rho GTP-Binding Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Xenopus Rnd1 and Rnd3 GTP-binding proteins are expressed under the control of segmentation clock and required for somite formation.
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pubmed:affiliation |
Division of Morphogenesis, National Institute for Basic Biology, Myodaiji, Okazaki, Japan. tg8j@cms.mail.virginia.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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