ArticleProtein science : a publication of the Protein Society2006
Molecular dynamics and in vitro analysis of Connexin43: A new 14-3-3 mode-1 interacting protein.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Functional 14-3-3 Proteins: Master Regulators in Plant Responses to Salt Stress.Plants (Basel, Switzerland) · 2025Review
- Review
- Role of Connexin 43 phosphorylation on Serine-368 by PKC in cardiac function and disease.Frontiers in cardiovascular medicine · 2022Review
- Impaired Cx43 gap junction endocytosis causes morphological and functional defects in zebrafish.Molecular biology of the cell · 2021Article
- Phosphorylation of Connexin36 near the C-terminus switches binding affinities for PDZ-domain and 14-3-3 proteins in vitro.Scientific reports · 2020Article
- Phosphorylation of cardiac voltage-gated sodium channel: Potential players with multiple dimensions.Acta physiologica (Oxford, England) · 2019Review
- Protein⁻Protein Interactions with Connexin 43: Regulation and Function.International journal of molecular sciences · 2018Review
- Phosphorylation regulates connexin43/ZO-1 binding and release, an important step in gap junction turnover.Molecular biology of the cell · 2017Article
- Progesterone Via its Type-A Receptor Promotes Myometrial Gap Junction Coupling.Scientific reports · 2017Article
- mTOR Regulates Gap Junction Alpha-1 Protein Trafficking in Sertoli Cells and Is Required for the Maintenance of Spermatogenesis in Mice.Biology of reproduction · 2016Article
- Molecular mechanisms regulating formation, trafficking and processing of annular gap junctions.BMC cell biology · 2016Review
- Proteomic Analysis of Connexin 43 Reveals Novel Interactors Related to Osteoarthritis.Molecular & cellular proteomics : MCP · 2015Article
- A 14-3-3 mode-1 binding motif initiates gap junction internalization during acute cardiac ischemia.Traffic (Copenhagen, Denmark) · 2014Article
- Cardiac to cancer: connecting connexins to clinical opportunity.FEBS letters · 2014Review
- 14-3-3θ facilitates plasma membrane delivery and function of mechanosensitive connexin 43 hemichannels.Journal of cell science · 2014Article
- Effects of phosphorylation on the structure and backbone dynamics of the intrinsically disordered connexin43 C-terminal domain.The Journal of biological chemistry · 2013Article
- Proteins and mechanisms regulating gap-junction assembly, internalization, and degradation.Physiology (Bethesda, Md.) · 2013Review
- The connexin43 carboxyl terminus and cardiac gap junction organization.Biochimica et biophysica acta · 2012Review
- CONNEXIN 43 AND BONE: NOT JUST A GAP JUNCTION PROTEIN.Actualizaciones en osteologia · 2011Article
- Effects of ethanol on the proteasome interacting proteins.World journal of gastroenterology · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The interaction of cellular proteins with the gap junction protein Connexin43 (Cx43) is thought to form a dynamic scaffolding complex that functions as a platform for the assembly of signaling, structural, and cytoskeletal proteins. A high stringency Scansite search of rat Cx43 identified the motif containing Ser373 (S373) as a 14-3-3 binding site. The S373 motif and the second best mode-1 motif, containing Ser244 (S244), are conserved in rat, mouse, human, chicken, and bovine, but not in Xenopus or zebrafish Cx43. Docking studies of a mouse/rat 14-3-3 homology model with the modeled phosphorylated S373 or S244 peptide ligands or their serine-to-alanine mutants, S373A or S244A, revealed that the pS373 motif facilitated a greater number of intermolecular contacts than the pS244 motif, thus supporting a stronger 14-3-3 binding interaction with the pS373 motif. The alanine substitution also reduced more than half the number of intermolecular contacts between 14-3-3 and the S373 motif, emphasizing the phosphorylation dependence of this interaction. Furthermore, the ability of the wild-type or the S244A GST-Cx43 C-terminal fusion protein, but not the S373A fusion protein, to interact with either 14-3-3 or 14-3-3zeta in GST pull-down experiments clearly demonstrated that the S373 motif mediates the direct interaction between Cx43 and 14-3-3 proteins. Blocking growth factor-induced Akt activation and presumably any Akt-mediated phosphorylation of the S373 motif in ROSE 199 cells did not prevent the down-regulation of Cx43-mediated cell-cell communication, suggesting that an Akt-mediated interaction with 14-3-3 was not involved in the disruption of Cx43 function.
Indexed as
Identifiers
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.