ArticleThe Journal of biological chemistry2009
The N terminus of connexin37 contains an alpha-helix that is required for channel function.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- A mechanism of CALHM1 ion channel gating.American journal of physiology. Cell physiology · 2025Article
- Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids.Science advances · 2020Article
- Connexins: Synthesis, Post-Translational Modifications, and Trafficking in Health and Disease.International journal of molecular sciences · 2018Review
- A structural and functional comparison of gap junction channels composed of connexins and innexins.Developmental neurobiology · 2017Review
- Gap junction structure: unraveled, but not fully revealed.F1000Research · 2017Review
- Specificity of the connexin W3/4 locus for functional gap junction formation.Channels (Austin, Tex.) · 2016Article
- Syndromic deafness mutations at Asn 14 differentially alter the open stability of Cx26 hemichannels.The Journal of general physiology · 2016Article
- Determinants of Cx43 Channel Gating and Permeation: The Amino Terminus.Biophysical journal · 2016Article
- Simvastatin Sodium Salt and Fluvastatin Interact with Human Gap Junction Gamma-3 Protein.PloS one · 2016Article
- Interfering amino terminal peptides and functional implications for heteromeric gap junction formation.Frontiers in pharmacology · 2013Article
- Cataract-associated D3Y mutation of human connexin46 (hCx46) increases the dye coupling of gap junction channels and suppresses the voltage sensitivity of hemichannels.Journal of bioenergetics and biomembranes · 2012Article
- Structure and functional studies of N-terminal Cx43 mutants linked to oculodentodigital dysplasia.Molecular biology of the cell · 2012Article
- Structural organization of intercellular channels II. Amino terminal domain of the connexins: sequence, functional roles, and structure.Biochimica et biophysica acta · 2012Review
- Asymmetric configurations and N-terminal rearrangements in connexin26 gap junction channels.Journal of molecular biology · 2011Article
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Authors and funding
7 authors.
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Abstract
The cytoplasmic N-terminal domain of connexins has been implicated in multiple aspects of gap junction function, including connexin trafficking/assembly and channel gating. A synthetic peptide corresponding to the first 23 amino acids of human connexin37 was prepared, and circular dichroism and nuclear magnetic resonance studies showed that this N-terminal peptide was predominantly alpha-helical between glycine 5 and glutamate 16. The importance of this structure for localization of the protein at appositional membranes and channel function was tested by expression of site-directed mutants of connexin37 in which amino acids leucine 10 and glutamine 15 were replaced with prolines or alanines. Wild type connexin37 and both substitution mutants localized to appositional membranes between transfected HeLa cells. The proline mutant did not allow intercellular transfer of microinjected neurobiotin; the alanine mutant allowed transfer, but less extensively than wild type connexin37. When expressed alone in Xenopus oocytes, wild type connexin37 produced hemichannel currents, but neither of the double substitution mutants produced detectable currents. The proline mutant (but not the alanine mutant) inhibited co-expressed wild type connexin37. Taken together, our data suggest that the alpha-helical structure of the connexin37 N terminus may be dispensable for protein localization, but it is required for channel and hemichannel function.
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