ArticleThe Journal of biological chemistry2012
Characterization of the structure and intermolecular interactions between the connexin 32 carboxyl-terminal domain and the protein partners synapse-associated protein 97 and calmodulin.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 45 citations in OpenAlex.
- Activity-dependent COeLife · 2026Article
- Spastin-mediated severing of glutamylated microtubules controls cardiomyocyte coupling.Nature cardiovascular research · 2026Article
- The relationship between Connexin 43 (Cx43) and partner protein, human discs large homologue-1 (Dlg1) during wound closure in keratinocytes.Cell and tissue research · 2026Article
- History of Gap Junction Architecture and Potential Role of Calmodulin in Channel Arrays.International journal of molecular sciences · 2025Review
- Calcium Role in Gap Junction Channel Gating: Direct Electrostatic or Calmodulin-Mediated?International journal of molecular sciences · 2024Review
- The human discs large protein 1 interacts with and maintains connexin 43 at the plasma membrane in keratinocytes.Journal of cell science · 2023Article
- CaInternational journal of molecular sciences · 2023Article
- Morphological and Functional Colonic Defects Caused by a Mutated Thyroid Hormone Receptor α.Thyroid : official journal of the American Thyroid Association · 2023Article
- Calmodulin-Connexin Partnership in Gap Junction Channel Regulation-Calmodulin-Cork Gating Model.International journal of molecular sciences · 2021Review
- The Roles of Calmodulin and CaMKII in Cx36 Plasticity.International journal of molecular sciences · 2021Review
- Article
- Calmodulin-Cork Model of Gap Junction Channel Gating-One Molecule, Two Mechanisms.International journal of molecular sciences · 2020Review
- Calmodulin-Mediated Regulation of Gap Junction Channels.International journal of molecular sciences · 2020Review
- Regulation of Connexin32 by ephrin receptors and T-cell protein-tyrosine phosphatase.The Journal of biological chemistry · 2019Article
- Phosphorylation of Cx43 residue Y313 by Src contributes to blocking the interaction with Drebrin and disassembling gap junctions.Journal of molecular and cellular cardiology · 2019Article
- Acetylation of C-terminal lysines modulates protein turnover and stability of Connexin-32.BMC cell biology · 2018Article
- Connexin43 Carboxyl-Terminal Domain Directly Interacts with β-Catenin.International journal of molecular sciences · 2018Article
- Protein⁻Protein Interactions with Connexin 43: Regulation and Function.International journal of molecular sciences · 2018Review
- Intramolecular signaling in a cardiac connexin: Role of cytoplasmic domain dimerization.Journal of molecular and cellular cardiology · 2017Article
- Chemical shift assignments of the connexin37 carboxyl terminal domain.Biomolecular NMR assignments · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In Schwann cells, connexin 32 (Cx32) can oligomerize to form intracellular gap junction channels facilitating a shorter pathway for metabolite diffusion across the layers of the myelin sheath. The mechanisms of Cx32 intracellular channel regulation have not been clearly defined. However, Ca(2+), pH, and the phosphorylation state can regulate Cx32 gap junction channels, in addition to the direct interaction of protein partners with the carboxyl-terminal (CT) domain. In this study, we used different biophysical methods to determine the structure and characterize the interaction of the Cx32CT domain with the protein partners synapse-associated protein 97 (SAP97) and calmodulin (CaM). Our results revealed that the Cx32CT is an intrinsically disordered protein that becomes α-helical upon binding CaM. We identified the GUK domain as the minimal SAP97 region necessary for the Cx32CT interaction. The Cx32CT residues affected by the binding of CaM and the SAP97 GUK domain were determined as well as the dissociation constants for these interactions. We characterized three Cx32CT Charcot-Marie-Tooth disease mutants (R219H, R230C, and F235C) and identified that whereas they all formed functional channels, they all showed reduced binding affinity for SAP97 and CaM. Additionally, we report that in RT4-D6P2T rat schwannoma cells, Cx32 is differentially phosphorylated and exists in a complex with SAP97 and CaM. Our studies support the importance of protein-protein interactions in the regulation of Cx32 gap junction channels and myelin homeostasis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.