Document Detail


The E3 ubiquitin ligase GREUL1 anteriorizes ectoderm during Xenopus development.
MedLine Citation:
PMID:  12435366     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We have identified a family of RING finger proteins that are orthologous to Drosophila Goliath (G1, Gol). One of the members, GREUL1 (Goliath Related E3 Ubiquitin Ligase 1), can convert Xenopus ectoderm into XAG-1- and Otx2-expressing cells in the absence of both neural tissue and muscle. This activity, combined with the finding that XGREUL1 is expressed within the cement gland, suggests a role for GREUL1 in the generation of anterior ectoderm. Although GREUL1 is not a direct inducer of neural tissue, it can activate the formation of ectopic neural cells within the epidermis of intact embryos. This suggests that GREUL1 can sensitize ectoderm to neuralizing signals. In this paper, we provide evidence that GREUL1 is an E3 ubiquitin ligase. Using a biochemical assay, we show that GREUL1 catalyzes the addition of polyubiquitin chains. These events are mediated by the RING domain since a mutation in two of the cysteines abolishes ligase activity. Mutation of these cysteines also compromises GREUL1's ability to induce cement gland. Thus, GREUL1's RING domain is necessary for both the ubiquitination of substrates and for the conversion of ectoderm to an anterior fate.
Authors:
Annette G M Borchers; Andrew L Hufton; Adam G Eldridge; Peter K Jackson; Richard M Harland; Julie C Baker
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Developmental biology     Volume:  251     ISSN:  0012-1606     ISO Abbreviation:  Dev. Biol.     Publication Date:  2002 Nov 
Date Detail:
Created Date:  2002-11-18     Completed Date:  2002-12-12     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0372762     Medline TA:  Dev Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  395-408     Citation Subset:  IM    
Affiliation:
Department of Genetics, Stanford University, Stanford, CA 94305, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Ectoderm / physiology*
Epidermis / embryology
Ligases / analysis,  chemistry,  physiology*
Mice
Molecular Sequence Data
Ubiquitin-Protein Ligases
Xenopus / embryology*
Grant Support
ID/Acronym/Agency:
R01 HD 41557/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
EC 6.-/Ligases; EC 6.3.2.19/Ubiquitin-Protein Ligases

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


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