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Fusion of GFP to the carboxyl terminus of connexin43 increases gap junction size in HeLa cells.
Hunter, Andrew W; Jourdan, Jane; Gourdie, Robert G.
Affiliation
  • Hunter AW; Department of Cell Biology and Anatomy, Medical University of South Carolina, SC 29425, USA. huntera@musc.edu
Cell Commun Adhes ; 10(4-6): 211-4, 2003.
Article in En | MEDLINE | ID: mdl-14681018
ABSTRACT
The pattern of gap junctional coupling between cells is thought to be important for the proper function of many types of tissues. At present, little is known about the molecular mechanisms that control the size and distribution of gap junctions. We addressed this issue by expressing connexin43 (Cx43) constructs in HeLa cells, a connexin-deficient cell line. HeLa cells expressing exogenously introduced wild-type Cx43 formed small, punctate gap junctions. By contrast, cells expressing Cx43-GFP formed large, sheet-like gap junctions. These results suggest that the GFP tag, which is fused to the carboxyl terminus of Cx43, alters gap junction size by masking the carboxyl terminal amino acids of Cx43 that comprise a zonula occludins-1 (ZO-1) binding site. We are currently testing this hypothesis using deletion and dominant-negative constructs that directly target the interaction between Cx43 and ZO-1.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Recombinant Fusion Proteins / Gap Junctions / Connexin 43 / Luminescent Proteins Limits: Humans Language: En Journal: Cell Commun Adhes Year: 2003 Document type: Article Affiliation country: United States
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Collection: 01-internacional Database: MEDLINE Main subject: Recombinant Fusion Proteins / Gap Junctions / Connexin 43 / Luminescent Proteins Limits: Humans Language: En Journal: Cell Commun Adhes Year: 2003 Document type: Article Affiliation country: United States