Document Detail


Fusogenic activity of EFF-1 is regulated via dynamic localization in fusing somatic cells of C. elegans.
MedLine Citation:
PMID:  15753035     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Many animal tissues form via fusion of cells. Yet in all instances of developmental cell fusion, the mechanism underlying fusion of plasma membranes remains poorly understood. EFF-1 is required for most somatic cell fusions in C. elegans, and misexpressed EFF-1 alters the normal pattern of fusing hypodermal cells. However, the autonomous activity of EFF-1, the rules governing its specificity, and the mechanism of its action have not been examined. RESULTS: We show that EFF-1 acts as a cellular fusogen, capable of inducing fusion of virtually any somatic cells in C. elegans, yet targeted precisely to fusion-fated contacts during normal development. Misexpression of EFF-1 in early embryos causes fusion among groups of cells composed entirely of nonfusion-fated members. Measurements of cytoplasm diffusion in induced fusion events show that ectopic EFF-1 expression produces fusion pores similar to those in normal fusion events. GFP-labeled EFF-1 is specifically targeted to fusion-competent cell contacts via reciprocal localization to the touching membranes of EFF-1-expressing cells. EFF-1 function is also governed by intercellular barriers that prohibit cell fusion between distinct tissues. Analysis of mutant versions of EFF-1 indicates a novel mode of fusogenicity, employing neither a phospholipase active site nor hydrophobic fusion-peptide acting solely in pore formation. CONCLUSIONS: EFF-1 can confer potent fusogenic activity to nonfusing cell types. However, it is normally targeted only to fusion-fated cell borders via mutual interaction between EFF-1-expressing cells and relocalization to the plasma membrane. Because EFF-1 appears evolutionarily unique to nematodes, multiple mechanisms may have evolved for controlled plasma-membrane fusion in development.
Authors:
Jacob J del Campo; Eugene Opoku-Serebuoh; Ariel B Isaacson; Victoria L Scranton; Morgan Tucker; Min Han; William A Mohler
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Current biology : CB     Volume:  15     ISSN:  0960-9822     ISO Abbreviation:  Curr. Biol.     Publication Date:  2005 Mar 
Date Detail:
Created Date:  2005-03-08     Completed Date:  2005-06-07     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9107782     Medline TA:  Curr Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  413-23     Citation Subset:  IM    
Affiliation:
Department of Genetics and Developmental Biology, University of Connecticut Health Center, Farmington, CT 06030, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Motifs / physiology
Animals
Caenorhabditis elegans / embryology*,  metabolism
Caenorhabditis elegans Proteins / genetics,  metabolism*
Cell Adhesion / physiology
Cell Membrane / metabolism,  physiology*
Cell Membrane Permeability / physiology
Computational Biology
DNA Primers
Gene Components
Gene Expression Regulation, Developmental*
Green Fluorescent Proteins
Membrane Glycoproteins / genetics,  metabolism*
Models, Biological*
Mutagenesis, Site-Directed
Mutation / genetics
Plasmids / genetics
Transgenes / genetics
Grant Support
ID/Acronym/Agency:
HD43156/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Caenorhabditis elegans Proteins; 0/DNA Primers; 0/EFF-1 protein, C elegans; 0/Membrane Glycoproteins; 147336-22-9/Green Fluorescent Proteins

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


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