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2. Physical properties of the cytoplasm modulate the rates of microtubule polymerization and depolymerization.

Author

Molines, Arthur, Lemière, Joël, Gazzola, Morgan, Steinmark, Ida, Edrington, Claire, Hsu, Chieh-Ting, Real-Calderon, Paula, Suhling, Klaus, Goshima, Gohta, Holt, Liam, Thery, Manuel, Brouhard, Gary, and Chang, Fred

Subjects
crowding, cytoplasm, cytoskeleton dynamics, density, diffusion, fission yeast Schizosaccharomyces pombe, microtubules, mitosis, rheology, viscosity, Cell Nucleus, Cytoplasm, Interphase, Microtubules, Polymerization, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Spindle Apparatus
Abstract

The cytoplasm is a crowded, visco-elastic environment whose physical properties change according to physiological or developmental states. How the physical properties of the cytoplasm impact cellular functions in vivo remains poorly understood. Here, we probe the effects of cytoplasmic concentration on microtubules by applying osmotic shifts to fission yeast, moss, and mammalian cells. We show that the rates of both microtubule polymerization and depolymerization scale linearly and inversely with cytoplasmic concentration; an increase in cytoplasmic concentration decreases the rates of microtubule polymerization and depolymerization proportionally, whereas a decrease in cytoplasmic concentration leads to the opposite. Numerous lines of evidence indicate that these effects are due to changes in cytoplasmic viscosity rather than cellular stress responses or macromolecular crowding per se. We reconstituted these effects on microtubules in vitro by tuning viscosity. Our findings indicate that, even in normal conditions, the viscosity of the cytoplasm modulates the reactions that underlie microtubule dynamic behaviors.

Published
2022

9. Fat1 deletion promotes hybrid EMT state, tumour stemness and metastasis

Author

Pastushenko, Ievgenia, Mauri, Federico, Song, Yura, de Cock, Florian, Meeusen, Bob, Swedlund, Benjamin, Impens, Francis, Van Haver, Delphi, Opitz, Matthieu, Thery, Manuel, Bareche, Yacine, Lapouge, Gaelle, Vermeersch, Marjorie, Van Eycke, Yves-Rémi, Balsat, Cédric, Decaestecker, Christine, Sokolow, Youri, Hassid, Sergio, Perez-Bustillo, Alicia, Agreda-Moreno, Beatriz, Rios-Buceta, Luis, Jaen, Pedro, Redondo, Pedro, Sieira-Gil, Ramon, Millan-Cayetano, Jose F., Sanmatrtin, Onofre, D’Haene, Nicky, Moers, Virginie, Rozzi, Milena, Blondeau, Jeremy, Lemaire, Sophie, Scozzaro, Samuel, Janssens, Veerle, De Troya, Magdalena, Dubois, Christine, Pérez-Morga, David, Salmon, Isabelle, Sotiriou, Christos, Helmbacher, Francoise, and Blanpain, Cédric

Published
2021
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10. Confined migration: Microtubules control the cell rear.

Author

Thery, Manuel and Akhmanova, Anna

Subjects
*IMMIGRATION enforcement, *ACTOMYOSIN, *MICROTUBULES, *ACTIN
Abstract

Cell migration through complex 3D environments relies on the interplay between actin and microtubules. A new study shows that, when cells pass through narrow constrictions, CLASP-dependent microtubule stabilisation at the cell rear controls actomyosin contractility to enable nuclear translocation and preserve cell integrity. [ABSTRACT FROM AUTHOR]

Published
2024
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18. Microtubules under mechanical pressure can breach dense actin networks

Author

Gelin, Matthieu, primary, Schaeffer, Alexandre, additional, Gaillard, Jeremie, additional, Guerin, Christophe, additional, Vianay, Benoit, additional, Orhant-Prioux, Magali, additional, Braun, Marcus, additional, Leterrier, Christophe, additional, Blanchoin, Laurent, additional, and THERY, Manuel, additional

Published
2023
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19. Evidence of inter‐ and intra‐keloid heterogeneity through analysis of dermal fibroblasts: A new insight in deciphering keloid physiopathology

Author

Serror, Kévin, primary, Ferrero, Lauren, additional, Boismal, Françoise, additional, Sintes, Maxime, additional, Thery, Manuel, additional, Vianay, Benoit, additional, Henry, Emilie, additional, Gentien, David, additional, DE LA Grange, Pierre, additional, Boccara, David, additional, Mimoun, Maurice, additional, Bouaziz, Jean‐David, additional, Benssussan, Armand, additional, and Michel, Laurence, additional

Published
2023
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28. Physical properties of the cytoplasm modulate the rates of microtubule polymerization and depolymerization

Author

Molines, Arthur T., Lemière, Joë, Gazzola, Morgan, Steinmark, Ida Emilie, Edrington, Claire H., Hsu, Chieh-Ting, Real-Calderon, Paula, Suhling, Klaus, Goshima, Gohta, Holt, Liam J., Thery, Manuel, Brouhard, Gary J., Chang, Fred, Molines, Arthur T., Lemière, Joë, Gazzola, Morgan, Steinmark, Ida Emilie, Edrington, Claire H., Hsu, Chieh-Ting, Real-Calderon, Paula, Suhling, Klaus, Goshima, Gohta, Holt, Liam J., Thery, Manuel, Brouhard, Gary J., and Chang, Fred

Abstract

© The Author(s), 2022. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Molines, A. T., Lemière, J., Gazzola, M., Steinmark, I. E., Edrington, C. H., Hsu, C.-T., Real-Calderon, P., Suhling, K., Goshima, G., Holt, L. J., Thery, M., Brouhard, G. J., & Chang, F. Physical properties of the cytoplasm modulate the rates of microtubule polymerization and depolymerization. Developmental Cell, 57(4), (2022): 466-479.e6, https://doi.org/10.1016/j.devcel.2022.02.001., The cytoplasm is a crowded, visco-elastic environment whose physical properties change according to physiological or developmental states. How the physical properties of the cytoplasm impact cellular functions in vivo remains poorly understood. Here, we probe the effects of cytoplasmic concentration on microtubules by applying osmotic shifts to fission yeast, moss, and mammalian cells. We show that the rates of both microtubule polymerization and depolymerization scale linearly and inversely with cytoplasmic concentration; an increase in cytoplasmic concentration decreases the rates of microtubule polymerization and depolymerization proportionally, whereas a decrease in cytoplasmic concentration leads to the opposite. Numerous lines of evidence indicate that these effects are due to changes in cytoplasmic viscosity rather than cellular stress responses or macromolecular crowding per se. We reconstituted these effects on microtubules in vitro by tuning viscosity. Our findings indicate that, even in normal conditions, the viscosity of the cytoplasm modulates the reactions that underlie microtubule dynamic behaviors., This work was supported by grants to F.C. (NIH GM115185, NIH GM056836, NIH GM146438), to L.J.H. (American Cancer Society RSG-19-073-01-TBE, Pershing Square Sohn Cancer Award, Chan Zuckerberg Initiative, NIH GM132447 and NIH CA240765), to G.G. (JSPS KAKENHI 17H06471 and 18KK0202), to K.S. (UK’s Biotechnology and Biological Sciences Research Council (BBSRC) grant BB/R004803/1) and to M.T. (ERC Consolidator Grant 771599). I.E.S. was supported by King’s College London through a LIDo (London Interdisciplinary Doctoral programme) iCASE studentship.

Published
2022

31. Oncogene-like induction of cellular invasion from centrosome amplification

Author

Godinho, Susana A., Picone, Remigio, Burute, Mithila, Dagher, Regina, Su, Ying, Leung, Cheuk T., Polyak, Kornelia, Brugge, Joan S., Thery, Manuel, and Pellman, David

Subjects
Genetic aspects, Research, Health aspects, Genetic research, Cancer research, Tumors -- Genetic aspects, Centrosome -- Health aspects, Gene expression -- Research, Oncology, Experimental, Centrosomes -- Health aspects, Cancer -- Research
Abstract

The centrosome is the major microtubule-organizing centre in mammalian cells and comprises of a pair of centrioles surrounded by the pericentriolar material (5). Centrosome abnormalities, usually increased numbers, are common [...], Centrosome amplification has long been recognized as a feature of human tumours; however, its role in tumorigenesis remains unclear (1). Centrosome amplification is poorly tolerated by non-transformed cells and, in the absence of selection, extra centrosomes are spontaneously lost (2). Thus, the high frequency of centrosome amplification, particularly in more aggressive tumours (3), raises the possibility that extra centrosomes could, in some contexts, confer advantageous characteristics that promote tumour progression. Using a three-dimensional model system and other approaches to culture human mammary epithelial cells, we find that centrosome amplification triggers cell invasion. This invasive behaviour is similar to that induced by overexpression of the breast cancer oncogene ERBB2 (ref. 4) and indeed enhances invasiveness triggered by ERBB2. Our data indicate that, through increased centrosomal microtubule nucleation, centrosome amplification increases Rac1 activity, which disrupts normal cell-cell adhesion and promotes invasion. These findings demonstrate that centrosome amplification, a structural alteration of the cytoskeleton, can promote features of malignant transformation.

Published
2014
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37. Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends

Author

Peris, Leticia, Thery, Manuel, Faure, Julien, Saoudi, Yasmina, Lafanechere, Laurence, Chilton, John K., Gordon-Weeks, Phillip, Galjart, Niels, Bornens, Michel, Wordeman, Linda, Wehland, Juergen, Andrieux, Annie, and Job, Didier

Subjects
Tyrosine -- Research, Tubulins -- Research, Microtubules -- Research, Biological sciences
Abstract

Tubulin-tyrosine ligase (TTL), the enzyme that catalyzes the addition of a C-terminal tyrosine residue to [alpha]-tubulin in the tubulin tyrosination cycle, is involved in tumor progression and has a vital role in neuronal organization. We show that in mammalian fibroblasts, cytoplasmic linker protein (CLIP) 170 and other microtubule plus-end tracking proteins comprising a cytoskeleton-associated protein glycine-rich (CAP-Gly) microtubule binding domain such as CLIP-115 and p150 Glued, localize to the ends of tyrosinated microtubules but not to the ends of detyrosinated microtubules. In vitro, the head domains of CLIP-170 and of p150 Glued bind more efficiently to tyrosinated microtubules than to detyrosinated polymers. In TTL-null fibroblasts, tubulin detyrosination and CAP-Gly protein mislocalization correlate with defects in both spindle positioning during mitosis and cell morphology during interphase. These results indicate that tubulin tyrosination regulates microtubule interactions with CAP-Gly microtubule plus-end tracking proteins and provide explanations for the involvement of TTL in tumor progression and in neuronal organization.

Published
2006

39. Fat1 deletion promotes hybrid EMT state, tumour stemness and metastasis

Author

Pastushenko, Ievgenia, primary, Mauri, Federico, additional, Song, Yura, additional, de Cock, Florian, additional, Meeusen, Bob, additional, Swedlund, Benjamin, additional, Impens, Francis, additional, Van Haver, Delphi, additional, Opitz, Matthieu, additional, Thery, Manuel, additional, Bareche, Yacine, additional, Lapouge, Gaelle, additional, Vermeersch, Marjorie, additional, Van Eycke, Yves-Rémi, additional, Balsat, Cédric, additional, Decaestecker, Christine, additional, Sokolow, Youri, additional, Hassid, Sergio, additional, Perez-Bustillo, Alicia, additional, Agreda-Moreno, Beatriz, additional, Rios-Buceta, Luis, additional, Jaen, Pedro, additional, Redondo, Pedro, additional, Sieira-Gil, Ramon, additional, Millan-Cayetano, Jose F., additional, Sanmatrtin, Onofre, additional, D’Haene, Nicky, additional, Moers, Virginie, additional, Rozzi, Milena, additional, Blondeau, Jeremy, additional, Lemaire, Sophie, additional, Scozzaro, Samuel, additional, Janssens, Veerle, additional, De Troya, Magdalena, additional, Dubois, Christine, additional, Pérez-Morga, David, additional, Salmon, Isabelle, additional, Sotiriou, Christos, additional, Helmbacher, Francoise, additional, and Blanpain, Cédric, additional

Published
2020
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40. Physical properties of the cytoplasm modulate the rates of microtubule polymerization and depolymerization

Author

Molines, Arthur T., primary, Lemière, Joël, additional, Gazzola, Morgan, additional, Steinmark, Emilie I., additional, Edrington, Claire H., additional, Hsu, Chieh-Ting (Jimmy), additional, Suhling, Klaus, additional, Goshima, Gohta, additional, Holt, Liam J., additional, Thery, Manuel, additional, Brouhard, Gary. J., additional, and Chang, Fred, additional

Published
2020
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41. Fat1 deletion promotes hybrid EMT state, tumour stemness and metastasis.

Author

Pastushenko, Ievgenia, Mauri, Federico, Song, Yura, De Cock, Frédérique, Meeusen, Bob, Swedlund, Benjamin, Impens, Francis, Van Haver, Delphi, Opitz, Matthieu, Thery, Manuel, Bareche, Yacine, Lapouge, Gaëlle, Vermeersch, Marjorie, Van Eycke, Yves-Remi, Balsat, Cédric, Decaestecker, Christine, Sokolow, Youri, Hassid, Sergio, Perez-Bustillo, Alicia, Agreda-Moreno, Beatriz, Rios-Buceta, Luis, Jaen, Pedro, Redondo, Pedro, Sieira-Gil, Ramon, Millan-Cayetano, Jose JF, Sanmatrtin, Onofre, D'Haene, Nicky, Moers, Virginie, Rozzi, Milena, Blondeau, Jérémy, Lemaire, Sophie, Scozzaro, Samuel, Janssens, Veerle, De Troya, Magdalena, Dubois, Christine, Perez-Morga, David, Salmon, Isabelle, Sotiriou, Christos, Helmbacher, Françoise, Blanpain, Cédric, Pastushenko, Ievgenia, Mauri, Federico, Song, Yura, De Cock, Frédérique, Meeusen, Bob, Swedlund, Benjamin, Impens, Francis, Van Haver, Delphi, Opitz, Matthieu, Thery, Manuel, Bareche, Yacine, Lapouge, Gaëlle, Vermeersch, Marjorie, Van Eycke, Yves-Remi, Balsat, Cédric, Decaestecker, Christine, Sokolow, Youri, Hassid, Sergio, Perez-Bustillo, Alicia, Agreda-Moreno, Beatriz, Rios-Buceta, Luis, Jaen, Pedro, Redondo, Pedro, Sieira-Gil, Ramon, Millan-Cayetano, Jose JF, Sanmatrtin, Onofre, D'Haene, Nicky, Moers, Virginie, Rozzi, Milena, Blondeau, Jérémy, Lemaire, Sophie, Scozzaro, Samuel, Janssens, Veerle, De Troya, Magdalena, Dubois, Christine, Perez-Morga, David, Salmon, Isabelle, Sotiriou, Christos, Helmbacher, Françoise, and Blanpain, Cédric

Abstract

FAT1, which encodes a protocadherin, is one of the most frequently mutated genes in human cancers1-5. However, the role and the molecular mechanisms by which FAT1 mutations control tumour initiation and progression are poorly understood. Here, using mouse models of skin squamous cell carcinoma and lung tumours, we found that deletion of Fat1 accelerates tumour initiation and malignant progression and promotes a hybrid epithelial-to-mesenchymal transition (EMT) phenotype. We also found this hybrid EMT state in FAT1-mutated human squamous cell carcinomas. Skin squamous cell carcinomas in which Fat1 was deleted presented increased tumour stemness and spontaneous metastasis. We performed transcriptional and chromatin profiling combined with proteomic analyses and mechanistic studies, which revealed that loss of function of FAT1 activates a CAMK2-CD44-SRC axis that promotes YAP1 nuclear translocation and ZEB1 expression that stimulates the mesenchymal state. This loss of function also inactivates EZH2, promoting SOX2 expression, which sustains the epithelial state. Our comprehensive analysis identified drug resistance and vulnerabilities in FAT1-deficient tumours, which have important implications for cancer therapy. Our studies reveal that, in mouse and human squamous cell carcinoma, loss of function of FAT1 promotes tumour initiation, progression, invasiveness, stemness and metastasis through the induction of a hybrid EMT state., info:eu-repo/semantics/published

Published
2020

42. CLASP Mediates Microtubule Repair by Restricting Lattice Damage and Regulating Tubulin Incorporation

Author

Celbiologie, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Aher, Amol, Rai, Dipti, Schaedel, Laura, Gaillard, Jeremie, John, Karin, Liu, Qingyang, Altelaar, Maarten, Blanchoin, Laurent, Thery, Manuel, Akhmanova, Anna, Celbiologie, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Aher, Amol, Rai, Dipti, Schaedel, Laura, Gaillard, Jeremie, John, Karin, Liu, Qingyang, Altelaar, Maarten, Blanchoin, Laurent, Thery, Manuel, and Akhmanova, Anna

Published
2020

43. CLASP Mediates Microtubule Repair by Restricting Lattice Damage and Regulating Tubulin Incorporation

Author

Cell Biology, Neurobiology and Biophysics, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Aher, Amol, Rai, Dipti, Schaedel, Laura, Gaillard, Jeremie, John, Karin, Liu, Qingyang, Altelaar, Maarten, Blanchoin, Laurent, Thery, Manuel, Akhmanova, Anna, Cell Biology, Neurobiology and Biophysics, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Aher, Amol, Rai, Dipti, Schaedel, Laura, Gaillard, Jeremie, John, Karin, Liu, Qingyang, Altelaar, Maarten, Blanchoin, Laurent, Thery, Manuel, and Akhmanova, Anna

Published
2020

49. Stem Cell-Like Properties of CK2β-down Regulated Mammary Cells

Author

Duchemin-Pelletier, Eve, Baulard, Megghane, Spreux, Elodie, Prioux, Magali, Burute, Mithila, Mograbi, Baharia, Guyon, Laurent, Thery, Manuel, Cochet, Claude, Filhol, Odile, Transduction du signal : signalisation calcium, phosphorylation et inflammation, Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Biologie du Cancer et de l'Infection (BCI ), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Physiologie cellulaire et végétale (LPCV), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), CytoMorphoLab, Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Physiologie cellulaire et végétale (LPCV), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Recherche Agronomique (INRA)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), EMI 00-092, Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Biologie à Grande Échelle (BGE - UMR S1038), Compartimentation et dynamique cellulaires (CDC), Centre National de la Recherche Scientifique (CNRS)-Institut Curie-Université Pierre et Marie Curie - Paris 6 (UPMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Physiologie cellulaire et végétale [2016-2019] (LPCV [2016-2019]), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Physiologie cellulaire et végétale [2016-2019] (LPCV [2016-2019]), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Recherche Agronomique (INRA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), INSERM, CEA, Ligue Nationale contre le Cancer, Ligue Comite de la Loire, University Grenoble Alpes, Espoir Foundation, ANR [PCV-08 CoCCINet], Immunité muqueuse et vaccination, Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR50-Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA), Invasion mechanisms in angiogenesis and cancer (IMAC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Ligue Comité de la Loire, ANR-08-PCVI-0027,CoCCINet,Construction of Cell-Cell Interaction Networks(2008), Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-IFR50-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Martin-Laffon, Jacqueline, Programme interdiciplinaire en physique et chimie du vivant - Construction of Cell-Cell Interaction Networks - - CoCCINet2008 - ANR-08-PCVI-0027 - PCV - VALID, Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut National de la Santé et de la Recherche Médicale (INSERM), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-IFR50-Université Côte d'Azur (UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA)

Subjects
[SDV.EE.SANT]Life Sciences [q-bio]/Ecology, environment/Health, Epithelial to Mesenchymal Transition, EMT, [SDV.CAN]Life Sciences [q-bio]/Cancer, lcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogens, lcsh:RC254-282, Article, stem cell, breast cancer, [SDV.CAN] Life Sciences [q-bio]/Cancer, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], protein kinase CK2, [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], ComputingMilieux_MISCELLANEOUS, epithelial plasticity
Abstract

International audience; The ubiquitous protein kinase CK2 has been demonstrated to be overexpressed in a number of human tumours. This enzyme is composed of two catalytic alpha or alpha' subunits and a dimer of beta regulatory subunits whose expression levels are probably implicated in CK2 regulation. Several recent papers reported that unbalanced expression of CK2 subunits is sufficient to drive epithelial to mesenchymal transition, a process involved in cancer invasion and metastasis. Herein, through transcriptomic and miRNA analysis together with comparison of cellular properties between wild type and CK2 beta-knock-down MCF10A cells, we show that down-regulation of CK2 beta subunit in mammary epithelial cells induces the acquisition of stem cell-like properties associated with perturbed polarity, CD44(high)/CD24(low) antigenic phenotype and the ability to grow under anchorage-independent conditions. These data demonstrate that a CK2 beta level establishes a critical cell fate threshold in the control of epithelial cell plasticity. Thus, this regulatory subunit functions as a nodal protein to maintain an epithelial phenotype and its depletion drives breast cell stemness.

Published
2017
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