Differential Phosphorylation of the Gap Junction Protein Connexin43 in Junctional Communication-Competent and -Deficient Cell Lines

Connexin43 is a member of the highly homologous connexin family of gap junction proteins. We have studied how connexin monomers are assembled into functional gap junction plaques by examining the biosynthesis of connexin43 in cell types that differ greatly in their ability to form functional gap jun...

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Published inThe Journal of cell biology Vol. 111; no. 5; pp. 2077 - 2088
Main Authors Musil, Linda S., Cunningham, Bruce A., Edelman, Gerald M., Goodenough, Daniel A.
Format Journal Article
LanguageEnglish
Published New York, NY Rockefeller University Press 01.11.1990
The Rockefeller University Press
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Abstract Connexin43 is a member of the highly homologous connexin family of gap junction proteins. We have studied how connexin monomers are assembled into functional gap junction plaques by examining the biosynthesis of connexin43 in cell types that differ greatly in their ability to form functional gap junctions. Using a combination of metabolic radiolabeling and immunoprecipitation, we have shown that connexin43 is synthesized in gap junctional communication-competent cells as a 42-kD protein that is efficiently converted to a ∼46-kD species (connexin43- P2) by the posttranslational addition of phosphate. Surprisingly, certain cell lines severely deficient in gap junctional communication and known cell-cell adhesion molecules (S180 and L929 cells) also expressed 42-kD connexin43. Connexin43 in these communication-deficient cell lines was not, however, phosphorylated to the P2 form. Conversion of S180 cells to a communication-competent phenotype by transfection with a cDNA encoding the cell-cell adhesion molecule L-CAM induced phosphorylation of connexin43 to the P2 form; conversely, blocking junctional communication in ordinarily communication-competent cells inhibited connexin43- P2 formation. Immunohistochemical localization studies indicated that only communication-competent cells accumulated connexin43 in visible gap junction plaques. Together, these results establish a strong correlation between the ability of cells to process connexin43 to the P2 form and to produce functional gap junctions. Connexin43 phosphorylation may therefore play a functional role in gap junction assembly and/or activity.
AbstractList Connexin43 is a member of the highly homologous connexin family of gap junction proteins. We have studied how connexin monomers are assembled into functional gap junction plaques by examining the biosynthesis of connexin43 in cell types that differ greatly in their ability to form functional gap junctions. Using a combination of metabolic radiolabeling and immunoprecipitation, we have shown that connexin43 is synthesized in gap junctional communication-competent cells as a 42-kD protein that is efficiently converted to a approximately 46-kD species (connexin43-P2) by the posttranslational addition of phosphate. Surprisingly, certain cell lines severely deficient in gap junctional communication and known cell-cell adhesion molecules (S180 and L929 cells) also expressed 42-kD connexin43. Connexin43 in these communication-deficient cell lines was not, however, phosphorylated to the P2 form. Conversion of S180 cells to a communication-competent phenotype by transfection with a cDNA encoding the cell-cell adhesion molecule L-CAM induced phosphorylation of connexin43 to the P2 form; conversely, blocking junctional communication in ordinarily communication-competent cells inhibited connexin43-P2 formation. Immunohistochemical localization studies indicated that only communication-competent cells accumulated connexin43 in visible gap junction plaques. Together, these results establish a strong correlation between the ability of cells to process connexin43 to the P2 form and to produce functional gap junctions. Connexin43 phosphorylation may therefore play a functional role in gap junction assembly and/or activity.
Connexin43 is a member of the highly homologous connexin family of gap junction proteins. We have studied how connexin monomers are assembled into functional gap junction plaques by examining the biosynthesis of connexin43 in cell types that differ greatly in their ability to form functional gap junctions. Using a combination of metabolic radiolabeling and immunoprecipitation, we have shown that connexin43 is synthesized in gap junctional communication-competent cells as a 42-kD protein that is efficiently converted to a ∼46-kD species (connexin43- P2) by the posttranslational addition of phosphate. Surprisingly, certain cell lines severely deficient in gap junctional communication and known cell-cell adhesion molecules (S180 and L929 cells) also expressed 42-kD connexin43. Connexin43 in these communication-deficient cell lines was not, however, phosphorylated to the P2 form. Conversion of S180 cells to a communication-competent phenotype by transfection with a cDNA encoding the cell-cell adhesion molecule L-CAM induced phosphorylation of connexin43 to the P2 form; conversely, blocking junctional communication in ordinarily communication-competent cells inhibited connexin43- P2 formation. Immunohistochemical localization studies indicated that only communication-competent cells accumulated connexin43 in visible gap junction plaques. Together, these results establish a strong correlation between the ability of cells to process connexin43 to the P2 form and to produce functional gap junctions. Connexin43 phosphorylation may therefore play a functional role in gap junction assembly and/or activity.
Author Edelman, Gerald M.
Cunningham, Bruce A.
Goodenough, Daniel A.
Musil, Linda S.
Author_xml – sequence: 1
  givenname: Linda S.
  surname: Musil
  fullname: Musil, Linda S.
– sequence: 2
  givenname: Bruce A.
  surname: Cunningham
  fullname: Cunningham, Bruce A.
– sequence: 3
  givenname: Gerald M.
  surname: Edelman
  fullname: Edelman, Gerald M.
– sequence: 4
  givenname: Daniel A.
  surname: Goodenough
  fullname: Goodenough, Daniel A.
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Issue 5
Keywords Immunohistochemistry
Phosphorylation
Gel electrophoresis
Rodentia
Biosynthesis
Gap junction
Posttranslational modification
Proteins
Vertebrata
Immunoprecipitation reaction
Mammalia
Cell line
Localization
Pulse labelling
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PublicationTitle The Journal of cell biology
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Snippet Connexin43 is a member of the highly homologous connexin family of gap junction proteins. We have studied how connexin monomers are assembled into functional...
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SubjectTerms Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Cell Adhesion Molecules - physiology
Cell communication
Cell Communication - physiology
Cell culture techniques
Cell Line
Cell lines
Cells
Cellular immunity
Connexins
Epithelial cells
Fundamental and applied biological sciences. Psychology
Gap junctions
Hepatocytes
Intercellular Junctions - chemistry
Intercellular Junctions - physiology
Membrane Proteins - biosynthesis
Membrane Proteins - metabolism
Miscellaneous
Phosphorylation
Protein Processing, Post-Translational
Proteins
Transfection
Title Differential Phosphorylation of the Gap Junction Protein Connexin43 in Junctional Communication-Competent and -Deficient Cell Lines
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https://www.ncbi.nlm.nih.gov/pubmed/2172261
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Volume 111
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