Document Detail

The second PDZ domain of zonula occludens-1 is dispensable for targeting to connexin 43 gap junctions.
MedLine Citation:
PMID:  18649178     Owner:  NLM     Status:  MEDLINE    
Zonula occludens (ZO)-1 is emerging as a central player in the control of gap junction (GJ) dynamics. Previously the authors reported that ZO-1 localizes preferentially to the periphery of Cx43 GJs. How ZO-1 arrives at GJ edges is unknown, but this targeting might involve we established interaction between the Cx43 C-terminus and the PDZ2 domain of ZO-1. Here the show that despite blocking the canonical PDZ2-mediated interaction by fusion of GFP to the C-terminus of Cx43, ZO-1 continued to target to domains juxtaposed with the edges of GJs comprised solely of tagged Cx43. This edge-association was not abolished by deletion of PDZ2 from ZO-1, as mutant ZO-1 also targeted to the periphery of GJs composed of either tagged or untagged Cx43. Additionally, ZO-2 was found colocalized with ZO-1 at GJ edges. These data demonstrate that ZO-1 targets to GJ edges independently of several known PDZ2-mediated interactions, including ZO-1 homodimerization, heterodimerization with ZO-2, and direct ZO-1 binding to the C-terminal residues of Cx43.
Andrew W Hunter; Robert G Gourdie
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Cell communication & adhesion     Volume:  15     ISSN:  1543-5180     ISO Abbreviation:  Cell Commun. Adhes.     Publication Date:  2008 May 
Date Detail:
Created Date:  2008-07-23     Completed Date:  2008-10-06     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101096596     Medline TA:  Cell Commun Adhes     Country:  United States    
Other Details:
Languages:  eng     Pagination:  55-63     Citation Subset:  IM    
Department of Cell Biology and Anatomy, Cardiovascular Developmental Biology Center, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
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MeSH Terms
Connexin 43 / metabolism*
Gap Junctions / metabolism*
Hela Cells
Membrane Proteins / physiology*
Phosphoproteins / physiology*
Protein Structure, Tertiary
Protein Transport / physiology
Tight Junctions / physiology
Grant Support
Reg. No./Substance:
0/Connexin 43; 0/Membrane Proteins; 0/Phosphoproteins; 0/zonula occludens-1 protein

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