Tyrosine Phosphorylation of Connexin 43 by v-Src Is Mediated by SH2 and SH3 Domain Interactions*
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Summary
Evidence is presented that the SH3 and SH2 domains of v-Src bind to proline-rich motifs and a phosphorylated tyrosine residue in the C-terminal tail of Cx43, providing further evidence for the direct involvement of v -Src in tyrosinesine phosphorylation of C x43 and inhibition of gap junctional communication in v-src-transformed cells.
- Type
- article
- Published
- 1997-09-05
- Cited by
- 185
- References
- 96
- Access
- Open access
- OpenAlex
- https://openalex.org/W1965028277
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19497097
Keywords
SH2 domain, Proto-oncogene tyrosine-protein kinase Src, SH3 domain, Tyrosine, Tyrosine phosphorylation
References
- Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells.
- An 81 kd protein complexed with middle T antigen and pp60c-src: a possible phosphatidylinositol kinase.
- Structure of gap junction intercellular channels.
- Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries.
- A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV‐1 Nef protein.
- The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.
- Activation of the oncogenic potential of the avian cellular src protein by specific structural alteration of the carboxy terminus.
- Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra‐ and intermolecular interactions.
- Subtype‐specific regulation of recombinant NMDA receptor‐channels by protein tyrosine kinases of the src family.
- Csk inhibition of c‐Src activity requires both the SH2 and SH3 domains of Src.
- Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells.
- Phospholipase C-gamma 1 associates with viral and cellular src kinases.
- Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates.
- Mutations in the SH3 domain of the src oncogene which decrease association of phosphatidylinositol 3'-kinase activity with pp60v-src and alter cellular morphology
- The purified product of the transforming gene of avian sarcoma virus phosphorylates tyrosine.
- A mutation in v-src that removes a single conserved residue in the SH-2 domain of pp60v-src restricts transformation in a host-dependent manner
- Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src
- Polyomavirus middle T antigen downregulates junctional cell-to-cell communication
- Low level of cellular protein phosphorylation by nontransforming overproduced p60c-src
- A novel signaling molecule, p130, forms stable complexes in vivo with v‐Crk and v‐Src in a tyrosine phosphorylation‐dependent manner.
Cited by
- Identification of connexin-interacting proteins: application of the yeast two-hybrid screen.
- Emerging issues of connexin channels: biophysics fills the gap
- Src Utilizes Cas to Block Gap Junctional Communication Mediated by Connexin43*
- Localisation aberrante de la connexine 43 dans le cancer du testicule
- The Role of Connexin-Mediated Cell–Cell Communication in Breast Cancer Metastasis
- Phosphorylation of Ser-279/282 and Tyr-265 Positions on Cx43 as Possible Mediators of VEGF-165 Inhibition of Pregnancy-Adapted Ca2+ Burst Function in Ovine Uterine Artery Endothelial Cells
- Domaine juxta-membranaire de la connexine43 : Détermination par RMN en solution de la structure et de l’interaction avec la tubuline et les microtubules
- Cumulus-oocyte complex interactions during oocyte maturation.
- Cardiac connexins: genes to nexus.
- Electron cryo-crystallography of a recombinant cardiac gap junction channel.
- TLR2 Regulates Gap Junction Intercellular Communication in Airway Cells1
- VEGF transiently disrupts gap junctional communication in endothelial cells.
- v-Src SH3-enhanced Interaction with Focal Adhesion Kinase at β1 Integrin-containing Invadopodia Promotes Cell Invasion*
- Studies on the tumor promoting mechanism of hard and soft segment models of polyetherurethane: Tyr265 phosphorylation of connexin43 is a key step in the GJIC inhibitory reaction induced by polyetherurethane.
- Regulation of gap junctions by phosphorylation of connexins.
- The v-Src SH3 Domain Facilitates a Cell Adhesion-independent Association with Focal Adhesion Kinase*
- Reciprocal influence of connexins and apical junction proteins on their expressions and functions
- Gap junctional complexes: from partners to functions.
- Receptor-operated calcium influx mediated by protein tyrosine kinase pathways.
- p38/SAPK2 controls gap junction closure in astrocytes
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