Change in permeant size selectivity by phosphorylation of connexin 43 gap-junctional hemichannels by PKC

Xiaoyong Bao, Chang Lee Sung, Luis Reuss, Guillermo A. Altenberg

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

Gap-junctional channels, permeable to large hydrophilic solutes of up to Mr ≈ 1,000, are responsible for cell-to-cell communication. Phosphorylation of connexin 43 (Cx43) by PKC abolishes the permeability of gap-junctional channels and hemichannels to large hydrophilic solutes, but not to small inorganic ions. Here, we report on a methodology to produce purified hemichannels of controlled subunit composition and apply it to the generation of hemichannels with variable number of PKC-phosphorylated subunits. The subunit composition was determined by luminescence resonance energy transfer. We show that all Cx43 subunits in the hemichannel hexamer have to be phosphorylated to abolish sucrose (Mr 342) permeability. We also show that the hemichannel pores with all subunits phosphorylated by PKC have a sizable diameter, allowing for permeation of the small hydrophilic solute ethyleneglycol (Mr 62). These results indicate that phosphorylation of Cx43 by PKC alters the hemichannel size selectivity and explain why PKC activity affects dye transfer between cells without consistent effects on electrical communication.

Original languageEnglish (US)
Pages (from-to)4919-4924
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume104
Issue number12
DOIs
StatePublished - Mar 20 2007

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Connexin 43
Phosphorylation
Permeability
Energy Transfer
Luminescence
Cell Communication
Sucrose
Coloring Agents
Ions

Keywords

  • Luminescence energy transfer
  • Membrane protein
  • Transport

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Change in permeant size selectivity by phosphorylation of connexin 43 gap-junctional hemichannels by PKC. / Bao, Xiaoyong; Sung, Chang Lee; Reuss, Luis; Altenberg, Guillermo A.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, No. 12, 20.03.2007, p. 4919-4924.

Research output: Contribution to journalArticle

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AU - Bao, Xiaoyong

AU - Sung, Chang Lee

AU - Reuss, Luis

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N2 - Gap-junctional channels, permeable to large hydrophilic solutes of up to Mr ≈ 1,000, are responsible for cell-to-cell communication. Phosphorylation of connexin 43 (Cx43) by PKC abolishes the permeability of gap-junctional channels and hemichannels to large hydrophilic solutes, but not to small inorganic ions. Here, we report on a methodology to produce purified hemichannels of controlled subunit composition and apply it to the generation of hemichannels with variable number of PKC-phosphorylated subunits. The subunit composition was determined by luminescence resonance energy transfer. We show that all Cx43 subunits in the hemichannel hexamer have to be phosphorylated to abolish sucrose (Mr 342) permeability. We also show that the hemichannel pores with all subunits phosphorylated by PKC have a sizable diameter, allowing for permeation of the small hydrophilic solute ethyleneglycol (Mr 62). These results indicate that phosphorylation of Cx43 by PKC alters the hemichannel size selectivity and explain why PKC activity affects dye transfer between cells without consistent effects on electrical communication.

AB - Gap-junctional channels, permeable to large hydrophilic solutes of up to Mr ≈ 1,000, are responsible for cell-to-cell communication. Phosphorylation of connexin 43 (Cx43) by PKC abolishes the permeability of gap-junctional channels and hemichannels to large hydrophilic solutes, but not to small inorganic ions. Here, we report on a methodology to produce purified hemichannels of controlled subunit composition and apply it to the generation of hemichannels with variable number of PKC-phosphorylated subunits. The subunit composition was determined by luminescence resonance energy transfer. We show that all Cx43 subunits in the hemichannel hexamer have to be phosphorylated to abolish sucrose (Mr 342) permeability. We also show that the hemichannel pores with all subunits phosphorylated by PKC have a sizable diameter, allowing for permeation of the small hydrophilic solute ethyleneglycol (Mr 62). These results indicate that phosphorylation of Cx43 by PKC alters the hemichannel size selectivity and explain why PKC activity affects dye transfer between cells without consistent effects on electrical communication.

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