Thierry Coppola

Centre National de la Recherche Scientifique

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Jean Mazella

Institut de Pharmacologie Moléculaire et Cellulaire

Sophie Béraud-Dufour

Institut de Pharmacologie Moléculaire et Cellulaire

Romano Regazzi

University of Lausanne

Marc Borsotto

Institut de Pharmacologie Moléculaire et Cellulaire

Amar Abderrahmani

Université de Lille

Michel Lazdunski

Institut de Pharmacologie Moléculaire et Cellulaire

Catherine Heurteaux

Institut de Pharmacologie Moléculaire et Cellulaire

Christelle Devader

Centre National de la Recherche Scientifique

Fabienne Massa

Université Côte d'Azur

Annie Schmid‐Alliana

Inserm

Cooperative Institutions

Centre National de la Recherche Scientifique

Inserm

Institut de Pharmacologie Moléculaire et Cellulaire

Université Côte d'Azur

Institut de Biologie Valrose

Observatoire de la Côte d’Azur

University of Lausanne

Centre National pour la Recherche Scientifique et Technique (CNRST)

Université Paris Cité

Laboratoire d'Excellence Canaux Ioniques d'Intérêt Thérapeutique

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VAMP2, but Not VAMP3/Cellubrevin, Mediates Insulin-dependent Incorporation of GLUT4 into the Plasma Membrane of L6 Myoblasts

Molecular Biology of the Cell (2000)

Varinder K. Randhawa Philip J. Bilan Zayna A. Khayat Nicholas Daneman Zhi Liu

Like neuronal synaptic vesicles, intracellular GLUT4-containing vesicles must dock and fuse with the plasma membrane, thereby facilitating insulin-regulated glucose uptake into muscle and fat cells. GLUT4 colocalizes in part with the vesicle SNAREs VAMP2 and VAMP3. In this study, we used a single-cell fluorescence-based assay to compare the functional involvement of VAMP2 and VAMP3 in GLUT4 translocation. Transient transfection of proteolytically active tetanus toxin light chain cleaved both VAMP2 and VAMP3 proteins in L6 myoblasts stably expressing exofacially myc-tagged GLUT4 protein and inhibited insulin-stimulated GLUT4 translocation. Tetanus toxin also caused accumulation of the remaining C-terminal VAMP2 and VAMP3 portions in Golgi elements. This behavior was exclusive to these proteins, because the localization of intracellular myc-tagged GLUT4 protein was not affected by the toxin. Upon cotransfection of tetanus toxin with individual vesicle SNARE constructs, only toxin-resistant VAMP2 rescued the inhibition of insulin-dependent GLUT4 translocation by tetanus toxin. Moreover, insulin caused a cortical actin filament reorganization in which GLUT4 and VAMP2, but not VAMP3, were clustered. We propose that VAMP2 is a resident protein of the insulin-sensitive GLUT4 compartment and that the integrity of this protein is required for GLUT4 vesicle incorporation into the cell surface in response to insulin.

GLUT4

10.1091/mbc.11.7.2403

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Citations (119)

Neurotensin receptor-2 and -3 are crucial for the anti-apoptotic effect of neurotensin on pancreatic β-TC3 cells

The International Journal of Biochemistry & Cell Biology (2009)

Sophie Béraud-Dufour Thierry Coppola Fabienne Massa Jean Mazella

Neurotensin receptor

10.1016/j.biocel.2009.04.002

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Citations (39)

Review for "Evidence that the multiflorine derived substituted quinazolidine 55P0251 augments insulin secretion and lowers blood glucose, via antagonism at α <sub>2</sub> ‐adrenoceptors in mice"

Thierry Coppola

10.1111/dom.13895/v2/review2

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The death domain of Rab3 guanine nucleotide exchange protein in GDP/GTP exchange activity in living cells

Biochemical Journal (2002)

Thierry Coppola Véronique Perret-Menoud Sonia Gattesco Sarah Magnin Isabel Pombo

Rab3 GTPases regulate exocytosis of neurons, endocrine and exocrine cells. In the present paper, we report a system to measure the guanine nucleotide status of Rab3 proteins in living cells. The assay is based on the ability of the Rab3 interacting molecule RIM to extract selectively the GTP-bound form of Rab3. Using this system, we found that approx. 20% of wild-type Rab3A, -B, -C or -D transfected in the insulin-secreting cell line HIT-T15 is in the GTP-bound conformation. The pool of activated Rab3 is decreased under conditions that stimulate exocytosis or by co-expression of the Rab3 GTPase-activating protein. In contrast, co-expression of Mss4 or Rab3-GEP (guanine nucleotide exchange protein) increases by approx. 3-fold the GTP-bound pool of Rab3 isoforms. Rab3-GEP is very similar to MADD, a death domain-containing protein that associates with the type 1 tumour necrosis factor receptor. We observed that the death domain of Rab3-GEP is involved in intramolecular interactions and that deletions or mutations that affect this domain of the protein impair the nucleotide exchange activity towards Rab3. We propose that the death domain of Rab3-GEP acts as a molecular switch and co-ordinates multiple functions of the protein by exchanging its binding partners.

Rab

GTP-binding protein regulators

Small GTPase

10.1042/0264-6021:3620273

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Citations (49)

Antibodies reveal the cytolocalization and subunit structure of the 1,4-dihydropyridine component of the neuronal Ca2+ channel

Biochemical and Biophysical Research Communications (1986)

Annie Schmid‐Alliana Jacques Barhanin Christiane Mourre Thierry Coppola Marc Borsotto

Component (thermodynamics)

10.1016/s0006-291x(86)80276-5

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Citations (27)

Neurotensin-induced Erk1/2 phosphorylation and growth of human colonic cancer cells are independent from growth factors receptors activation

Biochemical and Biophysical Research Communications (2011)

Fabienne Massa Aurélie Tormo Sophie Béraud-Dufour Thierry Coppola Jean Mazella

Neurotensin receptor

10.1016/j.bbrc.2011.09.034

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Citations (20)

Sortilin derived propeptide regulation during adipocyte differentiation and inflammation

Biochemical and Biophysical Research Communications (2016)

Céline Hivelin Jean Mazella Thierry Coppola

3T3-L1

10.1016/j.bbrc.2016.10.139

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Citations (9)

Neurotensin protects pancreatic beta cells from apoptosis

The International Journal of Biochemistry & Cell Biology (2008)

Thierry Coppola Sophie Béraud-Dufour A. Antoine Jean‐Pierre Vincent Jean Mazella

Enteroendocrine cell

Staurosporine

Neurotensin receptor

10.1016/j.biocel.2008.03.015

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Citations (38)

Therapeutic potential of prenylated stilbenoid macasiamenene F through its anti-inflammatory and cytoprotective effects on LPS-challenged monocytes and microglia

Journal of Ethnopharmacology (2020)

Veronika Leláková Sophie Béraud-Dufour Jan Hošek Karel Šmejkal Vilailak Prachyawarakorn

10.1016/j.jep.2020.113147

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Citations (22)

Structure, Functional Expression, and Cerebral Localization of the Levocabastine-Sensitive Neurotensin/Neuromedin N Receptor from Mouse Brain

Journal of Neuroscience (1996)

Jean Mazella J. Botto Eric Guillemare Thierry Coppola Philippe Sarret

This work describes the cloning and expression of the levocabastine-sensitive neurotensin (NT) receptor from mouse brain. The receptor protein comprises 417 amino acids and bears the characteristics of G-protein-coupled receptors. This new NT receptor (NTR) type is 39% homologous to, but pharmacologically distinct from, the only other NTR cloned to date from the rat brain and the human HT29 cell line. When the receptor is expressed in Xenopus laevis oocytes, the H1 antihistaminic drug levocabastine, like NT and neuromedin N, triggers an inward current. The pharmacological properties of this receptor correspond to those of the low-affinity, levocabastine-sensitive NT binding site described initially in membranes prepared from rat and mouse brain. It is expressed maximally in the cerebellum, hippocampus, piriform cortex, and neocortex of adult mouse brain.

Neurotensin receptor

Nociceptin receptor

Neocortex

10.1523/jneurosci.16-18-05613.1996

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Citations (235)