Regulation of connexin 43-mediated gap junctional intercellular communication by Ca2+ in mouse epidermal cells is controlled by E-cadherin.

Jongen, W.M.F.; Fitzgerald, D J; Asamoto, Makoto; Piccoli, C.; Slaga, Thomas J.; Gros, Daniël; Takeichi, Masatoshi; Yamasaki, Hiroshi

doi:10.1083/jcb.114.3.545

Cited by 330 publications

(165 citation statements)

References 48 publications

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“…More recently, Musil and Goodenough (1991) showed that cx43 in the triton-insoluble fraction, which represents cx43 in the gap junctional plaques, exists mainly in the phosphorylated P2 form and that the phosphorylation takes place after cx43 incorporation into the (nonjunctional) membrane. This implies that (Loewenstein, 1967;Keane et al, 1988;Mege et al, 1988;Musil et al, 1990;Jongen et al, 1991).…”

Section: Discussionmentioning

confidence: 96%

Transcription of the gene for the gap junctional protein connexin43 and expression of functional cell-to-cell channels are regulated by cAMP.

Mehta

Yamamoto

Rose

1992

MBoC

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We investigated the mechanism by which cyclic AMP (cAMP) induces gap junctional communication via cell-to-cell channels in a communication-deficient rat Morris hepatoma cell line. We found that under basal conditions, the cells transcribe cx43 at a low level but do not transcribe cx26 or cx32. Elevation of intracellular cAMP, which induced communication, increased cx43 mRNA 15-to 40-fold and the rate of cx43 transcription 6-fold. Cx43 protein was detected by immunostaining in junctions of only those cells in which communication had been induced. We found the regulation by cAMP also in other cell lines; namely, in those with a low basal level of cx43 mRNA.

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Section: Discussionmentioning

confidence: 96%

Transcription of the gene for the gap junctional protein connexin43 and expression of functional cell-to-cell channels are regulated by cAMP.

Mehta

Yamamoto

Rose

1992

MBoC

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“…Alternatively, the presence of low levels of ZO-1 at the edge of Cx43-GFP plaques could result indirectly via macromolecular associations between GJs and other cell-cell junctions that incorporate ZO-1. Adherens junctions are logical candidates in this respect as they are known to play a pivotal role in GJ stability (Hertig et al 1996;Jongen et al 1991;Li et al 2005;Meyer et al 1992;Musil et al 1990;Wei et al 2005) and cadherin-associated catenin complexes have been shown to bind both Cx43 (Ai et al 2000;Wei et al 2005) and ZO-1 (Itoh et al 1997).…”

Section: Resultsmentioning

confidence: 99%

The Second PDZ Domain of Zonula Occludens-1 Is Dispensable for Targeting to Connexin43 Gap Junctions

Hunter

Gourdie

2008

Cell Communication & Adhesion

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Zonula occludens (ZO)-1 is emerging as a central player in the control of gap junction (GJ) dynamics. Previously the authors reported that ZO-1 localizes preferentially to the periphery of Cx43 GJs. How ZO-1 arrives at GJ edges is unknown, but this targeting might involve we established interaction between the Cx43 C-terminus and the PDZ2 domain of ZO-1. Here the show that despite blocking the canonical PDZ2-mediated interaction by fusion of GFP to the C-terminus of Cx43, ZO-1 continued to target to domains juxtaposed with the edges of GJs comprised solely of tagged Cx43. This edge-association was not abolished by deletion of PDZ2 from ZO-1, as mutant ZO-1 also targeted to the periphery of GJs composed of either tagged or untagged Cx43. Additionally, ZO-2 was found colocalized with ZO-1 at GJ edges. These data demonstrate that ZO-1 targets to GJ edges independently of several known PDZ2-mediated interactions, including ZO-1 homodimerization, heterodimerization with ZO-2, and direct ZO-1 binding to the C-terminal residues of Cx43.

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“…In contrast, the overall expression and distribution of Ecadherin (Fig. 6), which has been suggested to play a role in Cx43 assembly, perhaps by providing cell-cell adhesion necessary for gap junction formation, [28][29][30][31][32] does not differ between the parental and mutant cell types. Thus, as for transport proteins whose trafficking is altered in Trf1 cells, it appears as though connexin trafficking, but not that of E-cadherin, is affected.…”

Section: Discussionmentioning

confidence: 99%

Deficient assembly and function of gap junctions in Trf1, a trafficking mutant of the human liver-derived cell line HuH-7

et al. 1999

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Gap junctions are complexes between adjacent cells that are responsible for direct intercellular communication via passive diffusion of low-molecular-weight hydrophilic molecules. The proteins present in gap junctions are termed connexins, of which at least 16 distinct gene products are known to occur in vertebrate species. 1,2 Connexin proteins differ notably from other membrane proteins in lacking glycosylation and being localized primarily at appositional regions between coupled cells. While the pathways of biogenesis, trafficking, assembly, and turnover have not yet been completely elucidated, key features appear to be more similar than not to ''typical'' plasma membrane proteins. [3][4][5][6][7][8][9][10][11] In previous studies, biochemical analysis of secretory or trafficking mutants 12-14 has elucidated many features of these pathways. This approach for analysis of gap junction biology has not been pursued in vertebrate cell lines harboring similar mutations. Characterization of connexin trafficking in the membrane protein trafficking mutant, Trf1, was undertaken as a first step in combining biochemical and mutational approaches to analysis of connexin trafficking and assembly.The Trf1 cell line was isolated as a result of a dual selection protocol. 15 Endocytic activity of 2 different carbohydratespecific receptors of the human hepatoma cell line HuH-7 were simultaneously selected against using gelonin, an inhibitor of protein synthesis, conjugated to galactose-and mannoseterminating glycoproteins. Because there was no significant reciprocal inhibition between the mannose-and galactoseterminating glycoproteins and their respective gelonin conjugates, the mutation harbored by Trf1 cells appeared to affect a common step in their endocytic pathway. This pleiotropic phenotype was extended to other cell-surface membrane proteins, including the transferrin receptor and the phenylalanine transporter.The Trf1 mutation provided the first genetic evidence for the existence of different subpopulations (States 1 and 2) of the asialoglycoprotein receptor (ASGPR) as described by Weigel and Oka. 16 Originally based on the biphasic kinetics of ligand-receptor complex dissociation, numerous characteristics have since been described that differentiate the 2 ASGPR subpopulations and the proposed endocytic pathways that they mediate. 17 While no biochemical basis for this receptor dichotomy has been established, only State 2 receptors were shown to be susceptible to modulation by a wide variety of cell perturbants and altered metabolic states of the liver. 17 The proposed existence of 2 subpopulations of receptors is not limited to ASGPR and has been suggested for a wide variety of cell-surface receptors on different cell types. The low-density lipoprotein and mannose-6-P receptors on fibroblasts, the mannose receptor and ␣ 2 macroglobulin receptor on alveolar macrophages, and the transferrin receptor on K562 and HuH-7 cells all respond to cell perturbants by a partial reduction in their surface expression, suggesting Abb...

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Regulation of connexin 43-mediated gap junctional intercellular communication by Ca2+ in mouse epidermal cells is controlled by E-cadherin.

Cited by 330 publications

References 48 publications

Transcription of the gene for the gap junctional protein connexin43 and expression of functional cell-to-cell channels are regulated by cAMP.

Transcription of the gene for the gap junctional protein connexin43 and expression of functional cell-to-cell channels are regulated by cAMP.

The Second PDZ Domain of Zonula Occludens-1 Is Dispensable for Targeting to Connexin43 Gap Junctions

Deficient assembly and function of gap junctions in Trf1, a trafficking mutant of the human liver-derived cell line HuH-7

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