Protein–protein interactions with connexin 43

Regulation and function

Paul L Sorgen, Andrew J. Trease, Gaelle Spagnol, Mario Delmar, Morten S. Nielsen

Research output: Contribution to journalReview article

12 Citations (Scopus)

Abstract

Connexins are integral membrane building blocks that form gap junctions, enabling direct cytoplasmic exchange of ions and low-molecular-mass metabolites between adjacent cells. In the heart, gap junctions mediate the propagation of cardiac action potentials and the maintenance of a regular beating rhythm. A number of connexin interacting proteins have been described and are known gap junction regulators either through direct effects (e.g., kinases) or the formation of larger multifunctional complexes (e.g., cytoskeleton scaffold proteins). Most connexin partners can be categorized as either proteins promoting coupling by stimulating forward trafficking and channel opening or inhibiting coupling by inducing channel closure, internalization, and degradation. While some interactions have only been implied through co-localization using immunohistochemistry, others have been confirmed by biophysical methods that allow detection of a direct interaction. Our understanding of these interactions is, by far, most well developed for connexin 43 (Cx43) and the scope of this review is to summarize our current knowledge of their functional and regulatory roles. The significance of these interactions is further exemplified by demonstrating their importance at the intercalated disc, a major hub for Cx43 regulation and Cx43 mediated effects.

Original languageEnglish (US)
Article number1428
JournalInternational journal of molecular sciences
Volume19
Issue number5
DOIs
StatePublished - May 10 2018

Fingerprint

Connexin 43
Connexins
Gap Junctions
Proteins
proteins
Ion Exchange
Molecular mass
interactions
Scaffolds (biology)
Metabolites
Cytoskeleton
Scaffolds
rhythm
Action Potentials
hubs
metabolites
regulators
Ion exchange
Phosphotransferases
Immunohistochemistry

Keywords

  • Connexin
  • Gap junction
  • Intercalated disc
  • Intrinsically disordered protein
  • Post-translational modification
  • Protein–protein interaction

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

Cite this

Protein–protein interactions with connexin 43 : Regulation and function. / Sorgen, Paul L; Trease, Andrew J.; Spagnol, Gaelle; Delmar, Mario; Nielsen, Morten S.

In: International journal of molecular sciences, Vol. 19, No. 5, 1428, 10.05.2018.

Research output: Contribution to journalReview article

Sorgen, Paul L ; Trease, Andrew J. ; Spagnol, Gaelle ; Delmar, Mario ; Nielsen, Morten S. / Protein–protein interactions with connexin 43 : Regulation and function. In: International journal of molecular sciences. 2018 ; Vol. 19, No. 5.
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