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Article: Cooperative cell-cell actin network remodeling to perform Gap junction endocytosis.

Segretain, Dominique / Di Marco, Mathilde / Dufeu, Chloé / Carette, Diane / Trubuil, Alain / Pointis, Georges

2023 Volume 33, Issue 1, Page(s) 20

Abstract: Background: The endocytosis of Gap junction plaques (GJP) requires cytoskeletal forces to internalize such large membranous structures. Actin, which partners the connexin proteins constituting Gap junctions and is located close to Annular Gap Junctions ( ...

Abstract	Background: The endocytosis of Gap junction plaques (GJP) requires cytoskeletal forces to internalize such large membranous structures. Actin, which partners the connexin proteins constituting Gap junctions and is located close to Annular Gap Junctions (AGJ), could be actively involved in this physiological process. Results: Electron Microscopy and Light Microscopy images, associated with time-lapse analysis and 3D reconstruction, used at high resolution and enhanced using ImageJ based software analysis, revealed that: i) actin cables, originating from Donor cells, insert on the edge of GJP and contribute to their invagination, giving rise to AGJ, whereas actin cables on the Acceptor cell side of the plaque are not modified; ii) actin cables from the Donor cell are continuous with the actin network present over the entire GJP surface. These actin cables fuse at a single point distant from the plaque, which then detaches itself from the membrane, condensing to form an actin mass during the final internalization process; iii) the Acceptor cell participates in the last step of the endocytic invagination process by forming an annular actin structure known as an actin ring. Conclusions: Together, these data suggest that the endocytosis of GJP is an example of a unique cooperative mechanism between the Donor (the traction of its actin cables) and the Acceptor cells (forming the actin ring).
Language	English
Publishing date	2023-08-03
Publishing country	England
Document type	Journal Article
ZDB-ID	2732675-5
ISSN	2051-4190
ISSN	2051-4190
DOI	10.1186/s12610-023-00194-y
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Article: Connexin43: emerging role in erectile function.

Pointis, Georges

The international journal of biochemistry & cell biology

2006 Volume 38, Issue 10, Page(s) 1642–1646

Abstract: Connexins, that have their main function as part of gap junction channels, are proteins expressed in a large number of tissues such as endocrine, nervous, vascular, and muscular tissues. Gap junctions are implicated in tissue homeostasis and control of ... ...

Abstract	Connexins, that have their main function as part of gap junction channels, are proteins expressed in a large number of tissues such as endocrine, nervous, vascular, and muscular tissues. Gap junctions are implicated in tissue homeostasis and control of cell proliferation and differentiation. Interestingly, mutations of connexin genes have been reported in several human diseases (peripheral neuropathies, cardiovascular and dermatological diseases, hereditary cataract, and deafness) and altered expression of connexins have been associated with tumoral progression. Today, several lines of study argue for a critical role of gap junctions in corporal smooth muscle relaxation and erectile response. The present review highlights the emerging role of connexin43, one of these membranous proteins, in the physiology and physiopathology of human erectile function and its possible medical application.
MeSH term(s)	Connexin 43/agonists ; Connexin 43/genetics ; Connexin 43/physiology ; Erectile Dysfunction/genetics ; Erectile Dysfunction/metabolism ; Erectile Dysfunction/therapy ; Gap Junctions/metabolism ; Humans ; Male ; Penile Erection/genetics ; Protein Conformation
Chemical Substances	Connexin 43
Language	English
Publishing date	2006
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2006.03.007
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Article: Multiple and complex influences of connexins and pannexins on cell death.

Gilleron, Jérôme / Carette, Diane / Segretain, Dominique / Pointis, Georges

Biochimica et biophysica acta. Biomembranes

2017 Volume 1860, Issue 1, Page(s) 182–191

Abstract: Cell death is a fundamental process for organogenesis, immunity and cell renewal. During the last decades a broad range of molecular tools were identified as important players for several different cell death pathways (apoptosis, pyroptosis, necrosis, ... ...

Abstract	Cell death is a fundamental process for organogenesis, immunity and cell renewal. During the last decades a broad range of molecular tools were identified as important players for several different cell death pathways (apoptosis, pyroptosis, necrosis, autosis…). Aside from these direct regulators of cell death programs, several lines of evidence proposed connexins and pannexins as potent effectors of cell death. In the present review we discussed the potential roles played by connexins, pannexins and innexins in the different cell death programs at different scales from gap junction intercellular communication to protein-protein interactions. This article is part of a Special Issue entitled: Gap Junction Proteins edited by Jean Claude Herve.
MeSH term(s)	Animals ; Apoptosis ; Connexins/metabolism ; Humans ; Necrosis ; Pyroptosis
Chemical Substances	Connexins
Language	English
Publishing date	2017-06-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0005-2736 ; 0006-3002 ; 0005-2728 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0005-2736 ; 0006-3002 ; 0005-2728 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamem.2017.06.004
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Article ; Online: Effects of a mixture of low doses of atrazine and benzo[a]pyrene on the rat seminiferous epithelium either during or after the establishment of the blood-testis barrier in the rat seminiferous tubule culture model.

Durand, Philippe / Blondet, Antonine / Martin, Guillaume / Carette, Diane / Pointis, Georges / Perrard, Marie-Hélène

Toxicology in vitro : an international journal published in association with BIBRA

2019 Volume 62, Page(s) 104699

Abstract: Atrazine (ATZ), a widely used agricultural pesticide and benzo[a]pyrene (BaP), a ubiquitous environmental human carcinogen can induce alterations of spermatogenesis. In the present study, we showed first that our seminiferous tubule culture model, in ... ...

Abstract	Atrazine (ATZ), a widely used agricultural pesticide and benzo[a]pyrene (BaP), a ubiquitous environmental human carcinogen can induce alterations of spermatogenesis. In the present study, we showed first that our seminiferous tubule culture model, in bicameral chambers, allowed the settlement of the blood-testis barrier (BTB) in 8-day-old male rat cultures and the differentiation of spermatogonia into round spermatids.The effect of a mixture of 1 μg/L of ATZ and 1 μg/L of BaP was then investigated either during or after the establishment of the BTB by using 8- or 20-22-day-old rats. Cultures were performed over a 3-week period. Our results show that claudin-11 and connexin 43 two proteins of the BTB, were impaired by the mixture which also reduced the number of round spermatids (the direct precursors of spermatozoa), by targeting the middle to late pachytene spermatocytes. These effects were observed in 8- and 20-22-day -old rat seminiferous tubule cultures. However, the decrease of the number of round spermatids was faster and more marked in the 8-day- than in the 20-22-day -old rat seminiferous tubule cultures. Our study emphasizes the possible influence of the age of an individual on the effect of (a) toxicant(s) on spermatogenesis.
MeSH term(s)	Animals ; Atrazine/toxicity ; Benzo(a)pyrene/toxicity ; Blood-Testis Barrier/drug effects ; Cells, Cultured ; Environmental Pollutants/toxicity ; Herbicides/toxicity ; Male ; Organ Culture Techniques ; Rats ; Rats, Sprague-Dawley ; Seminiferous Epithelium/drug effects ; Seminiferous Tubules/drug effects ; Spermatids/drug effects ; Spermatogenesis ; Spermatogonia/drug effects
Chemical Substances	Environmental Pollutants ; Herbicides ; Benzo(a)pyrene (3417WMA06D) ; Atrazine (QJA9M5H4IM)
Language	English
Publishing date	2019-11-02
Publishing country	England
Document type	Journal Article
ZDB-ID	639064-x
ISSN	1879-3177 ; 0887-2333
ISSN (online)	1879-3177
ISSN	0887-2333
DOI	10.1016/j.tiv.2019.104699
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Article ; Online: Connexin a check-point component of cell apoptosis in normal and physiopathological conditions.

Carette, Diane / Gilleron, Jérome / Chevallier, Daniel / Segretain, Dominique / Pointis, Georges

Biochimie

2014 Volume 101, Page(s) 1–9

Abstract: Gap junction protein connexins (Cxs) play essential roles in cell homeostasis, growth, differentiation and death. Therefore, Cx dysfunction has been associated with many diseases and with tumor development. Cxs control cell apoptosis through different ... ...

Abstract	Gap junction protein connexins (Cxs) play essential roles in cell homeostasis, growth, differentiation and death. Therefore, Cx dysfunction has been associated with many diseases and with tumor development. Cxs control cell apoptosis through different molecular mechanisms. First, gap junction channels classically facilitate the influx and flux of apoptotic signals between adjacent cells and hemichannels between the intracellular and extracellular environments. Second, recent studies demonstrate that Cx proteins, independently from their functional role through channels or hemichannels and in conjunction with their intracytoplasmic localization, may act as signaling effectors able to activate the canonical mitochondrial apoptotic pathway. In the present review, we dissected both functions of Cx in apoptosis, providing new avenues for apoptosis-mediated cancer therapy.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Apoptosis ; Cell Cycle Checkpoints ; Connexins/physiology ; Gap Junctions/physiology ; Humans ; Mitochondria/metabolism ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Neoplasms/pathology
Chemical Substances	Antineoplastic Agents ; Connexins
Language	English
Publishing date	2014-06
Publishing country	France
Document type	Journal Article ; Review
ZDB-ID	120345-9
ISSN	1638-6183 ; 0300-9084
ISSN (online)	1638-6183
ISSN	0300-9084
DOI	10.1016/j.biochi.2013.11.015
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Article ; Online: Physiological roles of connexins and pannexins in reproductive organs.

Kibschull, Mark / Gellhaus, Alexandra / Carette, Diane / Segretain, Dominique / Pointis, Georges / Gilleron, Jerome

Cellular and molecular life sciences : CMLS

2015 Volume 72, Issue 15, Page(s) 2879–2898

Abstract: Reproductive organs are complex and well-structured tissues essential to perpetuate the species. In mammals, the male and female reproductive organs vary on their organization, morphology and function. Connectivity between cells in such tissues plays ... ...

Abstract	Reproductive organs are complex and well-structured tissues essential to perpetuate the species. In mammals, the male and female reproductive organs vary on their organization, morphology and function. Connectivity between cells in such tissues plays pivotal roles in organogenesis and tissue functions through the regulation of cellular proliferation, migration, differentiation and apoptosis. Connexins and pannexins can be seen as major regulators of these physiological processes. In the present review, we assembled several lines of evidence demonstrating that these two families of proteins are essential for male and female reproduction.
MeSH term(s)	Animals ; Connexins/metabolism ; Gap Junctions/metabolism ; Gap Junctions/physiology ; Humans ; Organogenesis/physiology ; Reproduction/physiology
Chemical Substances	Connexins
Language	English
Publishing date	2015-06-23
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-015-1965-4
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Article: Testicular connexin 43, a precocious molecular target for the effect of environmental toxicants on male fertility.

Pointis, Georges / Gilleron, Jérôme / Carette, Diane / Segretain, Dominique

Spermatogenesis

2011 Volume 1, Issue 4, Page(s) 303–317

Abstract: Many recent epidemiological, clinical and experimental findings support the hypothesis that environmental toxicants are responsible for the increasing male reproductive disorders (congenital malformations, declining sperm counts and testicular cancer) ... ...

Abstract	Many recent epidemiological, clinical and experimental findings support the hypothesis that environmental toxicants are responsible for the increasing male reproductive disorders (congenital malformations, declining sperm counts and testicular cancer) over the past 20 years. It has also been reported that exposure to these toxicants, during critical periods of development (fetal and neonatal), represents a more considerable risk for animals and humans than exposure during adulthood. However, the molecular targets for these chemicals have not been clearly identified. Recent studies showed that a family of transmembranous proteins, named connexins, regulates numerous physiological processes involved in testicular development and function, such as Sertoli and germ cell proliferation, differentiation, germ cell migration and apoptosis. In the testis, knockout strategy revealed that connexin 43, the predominant connexin in this organ, is essential for spermatogenesis. In addition, there is evidence that many environmental toxicants could alter testicular connexin 43 by dysregulation of numerous mechanisms controlling its function. In the present work, we propose first to give an overview of connexin expression and intercellular gap junction coupling in the developing fetal and neonatal testes. Second, we underline the impact of maternally chemical exposure on connexin 43 expression in the perinatal developing testis. Lastly, we attempt to link this precocious effect to male offspring fertility.
Language	English
Publishing date	2011-10-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2629571-4
ISSN	2156-5562 ; 2156-5554
ISSN (online)	2156-5562
ISSN	2156-5554
DOI	10.4161/spmg.1.4.18392
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Article ; Online: New cellular mechanisms of gap junction degradation and recycling.

Carette, Diane / Gilleron, Jérôme / Denizot, Jean-Pierre / Grant, Kirsty / Pointis, Georges / Segretain, Dominique

Biology of the cell

2015 Volume 107, Issue 7, Page(s) 218–231

Abstract: Background information: Connexins (Cxs), the constitutive proteins of gap junctions, are key actors of many physiological processes. Therefore, alterations of Cx expression and degradation lead to the development of physiopathological disorders. Because ...

Abstract	Background information: Connexins (Cxs), the constitutive proteins of gap junctions, are key actors of many physiological processes. Therefore, alterations of Cx expression and degradation lead to the development of physiopathological disorders. Because of the formation of a double membrane vesicle termed annular gap junction (AGJ), gap junction degradation is a unique physiological process for which many cellular aspects remain unclear. Results: By using a combination of time-lapse fluorescence microscopy and high-resolution transmission electron microscopy, we evidenced new specific cellular events concerning gap junction degradation and recycling. Indeed, by time lapse video microscopy we demonstrated, for the first time to our knowledge, that an entire AGJ can be fully recycled back to the plasma membrane. Moreover, we dissected the degradative processes of gap junction by electron microscopy approaches. Interestingly, in addition to canonical autophagy and heterophagy pathways, previously described, we discovered that both pathways could sometimes intermingle. Strikingly, our results also highlighted a new lysosome-based autophagy pathway that could play a pivotal role in common autophagy degradation. Conclusions: The present investigation reveals that AGJ degradation is a more complex process that it was previously thought. First, a complete recycling of the gap junction plaque after its internalisation could occur. Second, the degradation of this peculiar double membrane structure is possible through autophagy, heterophagy, hetero-autophagy or by lysosomal-based autophagy. Altogether, this work underlines novel aspects of gap junction degradation that could be extended to other cell biology processes.
MeSH term(s)	Autophagy/physiology ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Cell Membrane/ultrastructure ; Connexins/genetics ; Connexins/metabolism ; Gap Junctions/genetics ; Gap Junctions/metabolism ; Gap Junctions/ultrastructure ; HeLa Cells ; Humans ; Lysosomes/genetics ; Lysosomes/metabolism ; Lysosomes/ultrastructure ; Microscopy, Electron, Transmission ; Microscopy, Fluorescence ; Proteolysis
Chemical Substances	Connexins
Language	English
Publishing date	2015-07
Publishing country	England
Document type	Journal Article
ZDB-ID	245745-3
ISSN	1768-322X ; 0399-0311 ; 0248-4900
ISSN (online)	1768-322X
ISSN	0399-0311 ; 0248-4900
DOI	10.1111/boc.201400048
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Zs.A 758: Show issues

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Article ; Online: Effects of low doses of carbendazim or iprodione either separately or in mixture on the pubertal rat seminiferous epithelium: An ex vivo study.

Durand, Philippe / Martin, Guillaume / Blondet, Antonine / Gilleron, Jérôme / Carette, Diane / Janczarski, Stéphane / Christin, Emilie / Pointis, Georges / Perrard, Marie-Hélène

Toxicology in vitro : an international journal published in association with BIBRA

2017 Volume 45, Issue Pt 3, Page(s) 366–373

Abstract: It has been shown that non-cytotoxic doses of Carbendazim (CBZ), a broad-spectrum benzimidazole fungicide, possess endocrine-disrupting (androgen-like) actions, ex vivo, on the pubertal rat seminiferous epithelium. Iprodione (IPR), a dicarboximide ... ...

Abstract	It has been shown that non-cytotoxic doses of Carbendazim (CBZ), a broad-spectrum benzimidazole fungicide, possess endocrine-disrupting (androgen-like) actions, ex vivo, on the pubertal rat seminiferous epithelium. Iprodione (IPR), a dicarboximide fungicide, is also known to be an endocrine-disrupter (anti-androgen). The effect of a mixture of these two pesticides was investigated in the validated rat seminiferous tubule culture model. Cultures were performed in the absence or presence of CBZ 50nM or IPR 50nM either alone or in mixture (Mix), over a 3-week period. Mix exerted a dramatic effect on two proteins (Connexin 43 and Claudin-11) of the blood-testis barrier and possessed similar effects to IPR on some germ cell populations. The presence of IPR together with CBZ (Mix) cancelled the effect of CBZ on the increase of the androgen-dependent TP1 and TP2 mRNAs and on the decrease of ERα, ERβ mRNAs. Nevertheless, CBZ alone or IPR alone or Mix induced toxicity on spermatogenesis resulting in a decrease of round spermatids (the precursors of spermatozoa). These results strongly suggest that, even at these low concentrations, the effects of IPR and of CBZ are not solely dependent on their respective anti-androgenic and androgen-like effects and should involve several mechanisms of action.
MeSH term(s)	Aminoimidazole Carboxamide/analogs & derivatives ; Aminoimidazole Carboxamide/toxicity ; Animals ; Benzimidazoles/toxicity ; Blood-Testis Barrier/drug effects ; Carbamates/toxicity ; Cells, Cultured ; Claudins/biosynthesis ; Claudins/genetics ; Connexin 43/biosynthesis ; Connexin 43/genetics ; Endocrine Disruptors/toxicity ; Fungicides, Industrial/toxicity ; Gene Expression Regulation/drug effects ; Hydantoins/toxicity ; Male ; Rats ; Rats, Sprague-Dawley ; Seminiferous Epithelium/drug effects ; Sexual Maturation ; Spermatocytes/drug effects ; Spermatogenesis/drug effects
Chemical Substances	Benzimidazoles ; Carbamates ; Claudins ; Cldn11 protein, rat ; Connexin 43 ; Endocrine Disruptors ; Fungicides, Industrial ; Gja1 protein, rat ; Hydantoins ; Aminoimidazole Carboxamide (360-97-4) ; carbendazim (H75J14AA89) ; iprodione (S3AYV2A6EU)
Language	English
Publishing date	2017-05-30
Publishing country	England
Document type	Journal Article
ZDB-ID	639064-x
ISSN	1879-3177 ; 0887-2333
ISSN (online)	1879-3177
ISSN	0887-2333
DOI	10.1016/j.tiv.2017.05.022
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Article ; Online: Heteromeric connexin 43/connexin 33 complex endocytosis: a connexin phosphorylation independent mechanism.

Carette, Diane / Gilleron, Jérome / Segretain, Dominique / Pointis, Georges

Biochimie

2010 Volume 92, Issue 5, Page(s) 555–559

Abstract: The role of gap junctions in proliferation, differentiation and apoptosis has been recently highlighted. Nevertheless, the molecular mechanisms that control these physiological events by acting on gap junction channels are still unknown. We have recently ...

Abstract	The role of gap junctions in proliferation, differentiation and apoptosis has been recently highlighted. Nevertheless, the molecular mechanisms that control these physiological events by acting on gap junction channels are still unknown. We have recently demonstrated that heteromeric gap junction plaques composed by Cx43 and Cx33 are unstable at the cell boundary and are rapidly internalized by endocytosis. In the present study, we analyze the phosphorylation status of Cx43 in homomeric (Cx43/Cx43) and heteromeric (Cx33/Cx43) complexes and their association with the tyrosine kinase c-Src. Our data show that c-Src interaction and P2 phosphorylation of Cx43, which are essential for homomeric Cx43 complex endocytosis, were altered in the heteromeric Cx33/Cx43 complex: lack of association between Cx33 and activated c-Src and disappearance of the P2 phosphorylated Cx43 isoform. The present findings demonstrate that the interaction of Cx33 with Cx43 within a same heteromeric complex may conduce to channel instability through alteration of the phosphorylation status of Cx43 independently of the control of the c-Src kinase. The data described here emphasize a new mechanism of Cx43 internalization Src kinase-independent.
MeSH term(s)	Amino Acid Sequence ; Animals ; Blotting, Western ; Cell Line ; Connexin 43/chemistry ; Connexin 43/metabolism ; Connexins/chemistry ; Connexins/metabolism ; Endocytosis ; Fluorescent Antibody Technique ; Humans ; Immunoprecipitation ; Male ; Mice ; Molecular Sequence Data ; Phosphorylation ; Sequence Homology, Amino Acid ; Sertoli Cells/metabolism
Chemical Substances	Connexin 43 ; Connexins ; Gja6 protein, rat (145717-22-2)
Language	English
Publishing date	2010-05
Publishing country	France
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120345-9
ISSN	1638-6183 ; 0300-9084
ISSN (online)	1638-6183
ISSN	0300-9084
DOI	10.1016/j.biochi.2010.02.003
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