Protein–Protein Interactions with Connexin 43: Regulation and Function

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

doi:10.3390/ijms19051428

Cited by 106Connexins and lens biologyCardiac electrophysiology and arrhythmiasCongenital heart defects research

Protein–Protein Interactions with Connexin 43: Regulation and Function

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Sorgen, Paul L., Trease, Andrew J., Spagnol, Gaelle, Delmar, Mario, Nielsen, Morten S.·2018·International Journal of Molecular Sciences

DOI 10.3390/ijms19051428PMC PMC5983787

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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.

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The intrinsically disordered C-terminal domain of connexins (148 amino acids) determines whether the channel is open or closed.
“The intrinsically disordered C-terminal domain of connexins (148 amino acids) determines whether the channel is open or closed.”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [253]

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Activator of G Protein Signaling 8 (AGS8) Is Required for Hypoxia-induced Apoptosis of Cardiomyocytes
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A PKA-ezrin-connexin 43 signaling complex controls gap junction communication and thereby trophoblast cell fusion
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Trafficking and Recycling of the Connexin43 Gap Junction Protein during Mitosis
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Phosphorylation regulates connexin43/ZO-1 binding and release, an important step in gap junction turnover
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Cardiomyocyte-specific overexpression of the ubiquitin ligase Wwp1 contributes to reduction in Connexin 43 and arrhythmogenesis
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Characterization of the Structure and Intermolecular Interactions between the Connexin 32 Carboxyl-terminal Domain and the Protein Partners Synapse-associated Protein 97 and Calmodulin
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Protein Kinase Cδ-mediated Phosphorylation of Connexin43 Gap Junction Channels Causes Movement within Gap Junctions followed by Vesicle Internalization and Protein Degradation
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14-3-3θ Facilitates plasma membrane delivery and function of mechanosensitive connexin 43 hemichannels
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The TSG101 protein binds to connexins and is involved in connexin degradation
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Dynamics of astrocyte adhesion as analyzed by a combination of atomic force microscopy and immunocytochemistry. The involvement of actin filaments and connexin 43 in the early stage of adhesion.
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Connexin43 Functions as a Novel Interacting Partner of Heat Shock Cognate Protein 70
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Gap Junction and Purinergic P2 Receptor Proteins as a Functional Unit: Insights from Transcriptomics
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[106]Zheng Li. Li H. Spagnol G. Patel K. Sorgen P.L. Src phosphorylation of Cx43 residue Y313 contributes to inhibiting the interaction with Drebrin and gap junction disassembly J. Mol. Cell. Cardiol. (under review) PMC8961861 30448479
[114]Spagnol G. Trease A.J. Zheng Li. Phillips A. Sorgen P.L. Regulation of Connexin43 by the direct interaction with β-catenin Int. J. Mol. Sci. (under review)

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Authors: Sorgen, P. L., Trease, A. J., Spagnol, G., Delmar, M., & Nielsen, M. S.
Affiliations: University of Nebraska Medical Center (US)
Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198, USA
NYU Langone Health (US)
University of Copenhagen (DK)
Corresponding author: Nielsen, Morten S.
ORCID: Sorgen, Paul L.
Trease, Andrew J.
Delmar, Mario
Nielsen, Morten S.
Venue: International Journal of Molecular Sciences
Publisher: MDPI AG
Published: 2018-05-10
Volume: 19
Issue: 5
Pages: 1428
ISSN: 1422-0067 (ISSN-L)
DOI: 10.3390/ijms19051428
PMC: PMC5983787
OpenAlex: W2802676035
Cited by: 106
References: 184
Citations by year: 2026: 3 · 2025: 15 · 2024: 9 · 2023: 14 · 2022: 14 · 2021: 11 · 2020: 23 · 2019: 8 · 2018: 9
FWCI: 1.25
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: International Journal of Molecular Sciences (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Hjerteforeningen
National Institutes of Health (GM319613, GM103427, GM072631)
National Heart, Lung, and Blood Institute (R01HL136179, R01HL134328, R01HL131712)
National Institute of General Medical Sciences (P20GM103427, R01GM072631)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Connexins and lens biology
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Congenital heart defects research
Keywords: connexin 43, protein-protein interaction, gap junctions, connexin trafficking, channel gating, connexin degradation, intercalated discs, cardiac action potential propagation, cardiac electrophysiology
MeSH terms: Cell Communication, Cytoskeleton, Humans, Gap Junctions, Connexin 43, Nuclear Matrix-Associated Proteins, Biophysical Phenomena, Protein Interaction Maps

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Protein–Protein Interactions with Connexin 43: Regulation and Function

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