ArticleCell communication & adhesion
Connexin43 PDZ2 binding domain mutants create functional gap junctions and exhibit altered phosphorylation.
Article in Cell communication & adhesion. 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, 29 citations in OpenAlex.
- Interaction of α Carboxyl Terminus 1 Peptide With the Connexin 43 Carboxyl Terminus Preserves Left Ventricular Function After Ischemia-Reperfusion Injury.Journal of the American Heart Association · 2019Article
- Targeting MAPK phosphorylation of Connexin43 provides neuroprotection in stroke.The Journal of experimental medicine · 2019Article
- Connexin 43 gap junctions contribute to brain endothelial barrier hyperpermeability in familial cerebral cavernous malformations type III by modulating tight junction structure.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Connexins in Cardiovascular and Neurovascular Health and Disease: Pharmacological Implications.Pharmacological reviews · 2017Review
- Epithelial barrier assembly requires coordinated activity of multiple domains of the tight junction protein ZO-1.Journal of cell science · 2013Article
- Proteins and mechanisms regulating gap-junction assembly, internalization, and degradation.Physiology (Bethesda, Md.) · 2013Review
- Posttranslational modifications in connexins and pannexins.The Journal of membrane biology · 2012Review
- Discovering the molecular components of intercellular junctions--a historical view.Cold Spring Harbor perspectives in biology · 2009Review
- Reciprocal influence of connexins and apical junction proteins on their expressions and functions.Biochimica et biophysica acta · 2009Review
- Coxsackievirus and adenovirus receptor (CAR) mediates atrioventricular-node function and connexin 45 localization in the murine heart.The Journal of clinical investigation · 2008Article
- Gap junction remodelling in human heart failure is associated with increased interaction of connexin43 with ZO-1.Cardiovascular research · 2008Article
- ZO-1 is required for protein kinase C gamma-driven disassembly of connexin 43.Cellular signalling · 2007Article
- Molecular dynamics and in vitro analysis of Connexin43: A new 14-3-3 mode-1 interacting protein.Protein science : a publication of the Protein Society · 2006Article
- Akt phosphorylates Connexin43 on Ser373, a "mode-1" binding site for 14-3-3.Cell communication & adhesionArticle
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Connexin43 (Cx43) is the most abundantly expressed gap junction protein. The C-terminal tail of Cx43 is important for regulation of gap junctions via phosphorylation of specific tyrosine and serine residues and through interactions with cellular proteins. The C-terminus of Cx43 has been shown to interact with the PDZ2 domain of the tight and adherens junction associated zona occludens 1 (ZO-1) protein. Analysis of the PDZ2 binding domain of Cx43 indicated that positions -3 and -2, and the final hydrophobic amino acid at the C-terminus, are critical for ZO-1 binding. In addition, the C-termini of connexins 40 and 45, but not Cx32, interacted with ZO-1. To evaluate the functional significance of the Cx43-ZO-1 interaction, Cx43 wild type (Cx43wt) and mutants lacking either the C-terminal hydrophobic isoleucine (Cx43deltaI382) or the last five amino acids (Cx43delta378-382), required for ZO-1 binding in vitro, were introduced into a Cx43-deficient MDCK cell line. In vitro binding studies and coimmunoprecipitation assays indicated that these Cx43 mutants failed to interact with ZO-1. Confocal and deconvolution microscopy revealed that a fraction of Cx43wt colocalized with ZO-1 at the plasma membrane. A similar colocalization pattern was observed for the Cx43deltaI382 and Cx43 delta378-382 mutants, which were translocated to the plasma membrane and formed functional gap junction channels. The wt and mutant Cx43 appeared to have similar turnover rates. However, the P2 and P3 phosphoisoforms of the Cx43 mutants were significantly reduced compared to Cx43wt. These studies indicated that the interaction of Cx43 with ZO-1 may contribute to the regulation of Cx43 phosphorylation.
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