Document Detail


Rere controls retinoic acid signalling and somite bilateral symmetry.
MedLine Citation:
PMID:  20164929     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
One of the most notable features of the vertebrate body plan organization is its bilateral symmetry, evident at the level of vertebrae and skeletal muscles. Here we show that a mutation in Rere (also known as atrophin2) leads to the formation of asymmetrical somites in mouse embryos, similar to embryos deprived of retinoic acid. Furthermore, we also demonstrate that Rere controls retinoic acid signalling, which is required to maintain somite symmetry by interacting with Fgf8 in the left-right signalling pathway. Rere forms a complex with Nr2f2, p300 (also known as Ep300) and a retinoic acid receptor, which is recruited to the retinoic acid regulatory element of retinoic acid targets, such as the Rarb promoter. Furthermore, the knockdown of Nr2f2 and/or Rere decreases retinoic acid signalling, suggesting that this complex is required to promote transcriptional activation of retinoic acid targets. The asymmetrical expression of Nr2f2 in the presomitic mesoderm overlaps with the asymmetry of the retinoic acid signalling response, supporting its implication in the control of somitic symmetry. Misregulation of this mechanism could be involved in symmetry defects of the human spine, such as those observed in patients with scoliosis.
Authors:
Gon?alo C Vilhais-Neto; Mitsuji Maruhashi; Karen T Smith; Mireille Vasseur-Cognet; Andrew S Peterson; Jerry L Workman; Olivier Pourqui?
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Nature     Volume:  463     ISSN:  1476-4687     ISO Abbreviation:  Nature     Publication Date:  2010 Feb 
Date Detail:
Created Date:  2010-02-18     Completed Date:  2010-03-29     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  953-7     Citation Subset:  IM    
Affiliation:
Stowers Institute for Medical Research, Missouri 64110, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Body Patterning / physiology*
COUP Transcription Factor II / deficiency,  genetics,  metabolism
Cell Line
E1A-Associated p300 Protein / metabolism
Embryo, Mammalian / embryology,  metabolism
Fibroblast Growth Factor 8 / metabolism
Gene Expression Regulation, Developmental
Mice
Mice, Inbred C57BL
Multiprotein Complexes / chemistry,  metabolism
Nerve Tissue Proteins / deficiency,  genetics,  metabolism*
Promoter Regions, Genetic / genetics
Receptors, Retinoic Acid / genetics,  metabolism
Repressor Proteins / deficiency,  genetics,  metabolism*
Response Elements / genetics
Signal Transduction*
Somites / embryology*,  metabolism*
Tretinoin / metabolism*
Grant Support
ID/Acronym/Agency:
//Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/COUP Transcription Factor II; 0/Ep300 protein, mouse; 0/Fgf8 protein, mouse; 0/Multiprotein Complexes; 0/Nerve Tissue Proteins; 0/Nr2f2 protein, mouse; 0/Receptors, Retinoic Acid; 0/Repressor Proteins; 0/atrophin 2, mouse; 0/retinoic acid receptor beta; 148997-75-5/Fibroblast Growth Factor 8; 302-79-4/Tretinoin; EC 2.3.1.48/E1A-Associated p300 Protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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