Document Detail

A dominant negative mutation of neuronal connexin 36 that blocks intercellular permeability.
MedLine Citation:
PMID:  11834292     Owner:  NLM     Status:  MEDLINE    
Rat connexin 36 (Cx36) was mutated by substituting serine for cysteine at residue 231 (C231S) and the mutant's effect on the subcellular localization of wild-type Cx36 and the intercellular permeability that it confers was determined in human HeLa and rat PC12 cells. Cells transfected with the mutant or wild-type Cx36 cDNA expressed the expected 36 kDa protein and Cx36 immunoreactivity. Co-immunoprecipitation experiments with monkey COS-7 cells transiently transfected with both mutant and wild-type Cx36 cDNAs demonstrated that the mutant protein bound to the wild-type. Double immunofluorescence microscopy of stably transfected HeLa cells demonstrated that mutant Cx36 blocked the transport of the wild-type Cx36 to the cell membrane, primarily by trapping it in the endoplasmic reticulum around the nucleus. Coexpression of the mutant Cx36 with the wild-type protein abolished the ability of the latter to permit dye transfer in both HeLa and PC12 cells. The findings are the first demonstration of a mutation of Cx36 that inhibits wild-type Cx36 function in mammalian cells.
Dimitris Placantonakis; Federico Cicirata; John P Welsh
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Brain research. Molecular brain research     Volume:  98     ISSN:  0169-328X     ISO Abbreviation:  Brain Res. Mol. Brain Res.     Publication Date:  2002 Jan 
Date Detail:
Created Date:  2002-02-08     Completed Date:  2002-04-29     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8908640     Medline TA:  Brain Res Mol Brain Res     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  15-28     Citation Subset:  IM    
Department of Physiology and Neuroscience, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
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MeSH Terms
Amino Acid Substitution*
COS Cells / metabolism
Cell Communication / genetics*
Cercopithecus aethiops
Connexins / genetics*,  physiology
DNA, Complementary / genetics
Endoplasmic Reticulum / metabolism
Fluorescent Dyes / metabolism
Gap Junctions / metabolism*
Genes, Dominant
Golgi Apparatus / metabolism
Hela Cells / metabolism
Microscopy, Fluorescence
Mutagenesis, Site-Directed
Mutation, Missense*
Nerve Tissue Proteins / metabolism
Neurons / metabolism,  ultrastructure
PC12 Cells / metabolism
Point Mutation*
Protein Transport
Recombinant Fusion Proteins / physiology
Subcellular Fractions / metabolism
Grant Support
Reg. No./Substance:
0/Connexins; 0/DNA, Complementary; 0/Fluorescent Dyes; 0/Nerve Tissue Proteins; 0/Recombinant Fusion Proteins; 0/connexin 36

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

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