ArticleBiophysical journal2009
Calmodulin mediates the Ca2+-dependent regulation of Cx44 gap junctions.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed, 51 citations in OpenAlex.
- 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
- Calcium Regulation of Connexin Hemichannels.International journal of molecular sciences · 2024Review
- CaInternational journal of molecular sciences · 2023Article
- Calmodulin-Connexin Partnership in Gap Junction Channel Regulation-Calmodulin-Cork Gating Model.International journal of molecular sciences · 2021Review
- Structural Aspects and Prediction of Calmodulin-Binding Proteins.International journal of molecular sciences · 2020Review
- Regulation of Connexin Gap Junctions and Hemichannels by Calcium and Calcium Binding Protein Calmodulin.International journal of molecular sciences · 2020Review
- Article
- Calmodulin Binding to Connexin 35: Specializations to Function as an Electrical Synapse.International journal of molecular sciences · 2020Article
- Calmodulin-Cork Model of Gap Junction Channel Gating-One Molecule, Two Mechanisms.International journal of molecular sciences · 2020Review
- Design of Calcium-Binding Proteins to Sense Calcium.Molecules (Basel, Switzerland) · 2020Review
- Calmodulin-Mediated Regulation of Gap Junction Channels.International journal of molecular sciences · 2020Review
- Tubulin-Dependent Transport of Connexin-36 Potentiates the Size and Strength of Electrical Synapses.Cells · 2019Article
- Inner Ear Connexin Channels: Roles in Development and Maintenance of Cochlear Function.Cold Spring Harbor perspectives in medicine · 2019Review
- Calcium-calmodulin gating of a pH-insensitive isoform of connexin43 gap junctions.The Biochemical journal · 2019Article
- Cataract-associated connexin 46 mutation alters its interaction with calmodulin and function of hemichannels.The Journal of biological chemistry · 2018Article
- What's the Function of Connexin 32 in the Peripheral Nervous System?Frontiers in molecular neuroscience · 2018Review
- Direct visualization of interaction between calmodulin and connexin45.The Biochemical journal · 2017Article
- Focus on lens connexins.BMC cell biology · 2017Review
- Structural and Functional Consequences of Connexin 36 (Cx36) Interaction with Calmodulin.Frontiers in molecular neuroscience · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
We have shown previously that the Ca2+-dependent inhibition of lens epithelial cell-to-cell communication is mediated in part by the direct association of calmodulin (CaM) with connexin43 (Cx43), the major connexin in these cells. We now show that elevation of [Ca2+](i) in HeLa cells transfected with the lens fiber cell gap junction protein sheep Cx44 also results in the inhibition of cell-to-cell dye transfer. A peptide comprising the putative CaM binding domain (aa 129-150) of the intracellular loop region of this connexin exhibited a high affinity, stoichiometric interaction with Ca2+-CaM. NMR studies indicate that the binding of Cx44 peptide to CaM reflects a classical embracing mode of interaction. The interaction is an exothermic event that is both enthalpically and entropically driven in which electrostatic interactions play an important role. The binding of the Cx44 peptide to CaM increases the CaM intradomain cooperativity and enhances the Ca2+-binding affinities of the C-domain of CaM more than twofold by slowing the rate of Ca2+ release from the complex. Our data suggest a common mechanism by which the Ca2+-dependent inhibition of the alpha-class of gap junction proteins is mediated by the direct association of an intracellular loop region of these proteins with Ca2+-CaM.
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What OpenQuestion holds
Registered trials
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.