ArticleArchives of biochemistry and biophysics2012
Structural studies of N-terminal mutants of connexin 32 using (1)H NMR spectroscopy.
Article in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- The Complex and Critical Role of Glycine 12 (G12) in Beta-Connexins of Human Skin.International journal of molecular sciences · 2021Review
- What's the Function of Connexin 32 in the Peripheral Nervous System?Frontiers in molecular neuroscience · 2018Review
- Gating of Connexin Channels by transjunctional-voltage: Conformations and models of open and closed states.Biochimica et biophysica acta. Biomembranes · 2018Review
- Structural studies of N-terminal mutants of Connexin 26 and Connexin 32 using (1)H NMR spectroscopy.Archives of biochemistry and biophysics · 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
- Voltage regulation of connexin channel conductance.Yonsei medical journal · 2015Review
- Motifs in the permeation pathway of connexin channels mediate voltage and Ca (2+) sensing.Frontiers in physiology · 2014Review
- Proteins and mechanisms regulating gap-junction assembly, internalization, and degradation.Physiology (Bethesda, Md.) · 2013Review
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The amino terminus of gap junction proteins, connexins, plays a fundamental role in voltage gating and ion permeation. We have previously shown with (1)H NMR that the structure of the N-terminus of functional connexin molecules contains a flexible turn around G12 (Arch. Biochem. Biophys.490:9,2009) allowing the N-terminus to form a portion of the channel pore near the cytoplasmic entrance. The mutants of nonfunctional connexin molecules G12S and G12Y were found to prevent this turn. Previous functional studies of loci at which Cx32 mutations cause a peripheral neuropathy, Charcot-Marie-Tooth disease, have shown that G12S is not plasma membrane inserted. Presently, we solve the structure of nonfunctional Connexin 32 mutants W3D and Y7D which do not appear to be membrane inserted. Using 2D (1)H NMR, we report that similar to G12S and G12Y, alterations in hydrophobic sidechain interactions disrupt (Y7D) or constrain (W3D) the flexible turn around G12. The alteration in the open turn around residue 12, observed in all nonfunctional mutants G12S, G12Y, W3D and Y7D correlates with loss of function. We propose that loss of the open turn causes the N-terminus to extend out of the channel pore and this misfolding may target mutants for destruction in the endoplasmic reticulum.
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