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Article ; Online: Tension cellulaire et trafic des intégrines.

Bouin, Anne-Pascale / Kyumurkov, Alexander / Planus, Emmanuelle / Albiges-Rizo, Corinne

2023 Volume 39, Issue 8-9, Page(s) 597–599

Title translation	Cellular tension and integrin trafficking.
MeSH term(s)	Humans ; Integrins/metabolism ; Cell Movement ; Protein Transport ; Cell Adhesion
Chemical Substances	Integrins
Language	French
Publishing date	2023-09-11
Publishing country	France
Document type	Research Support, Non-U.S. Gov't ; News
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2023089
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Article: CK2β Is a Gatekeeper of Focal Adhesions Regulating Cell Spreading.

Filhol, Odile / Hesse, Anne-Marie / Bouin, Anne-Pascale / Albigès-Rizo, Corinne / Jeanneret, Florian / Battail, Christophe / Pflieger, Delphine / Cochet, Claude

Frontiers in molecular biosciences

2022 Volume 9, Page(s) 900947

Abstract: CK2 is a hetero-tetrameric serine/threonine protein kinase made up of two CK2α/α' catalytic subunits and two CK2β regulatory subunits. The free CK2α subunit and the tetrameric holoenzyme have distinct substrate specificity profiles, suggesting that the ... ...

Abstract	CK2 is a hetero-tetrameric serine/threonine protein kinase made up of two CK2α/α' catalytic subunits and two CK2β regulatory subunits. The free CK2α subunit and the tetrameric holoenzyme have distinct substrate specificity profiles, suggesting that the spatiotemporal organization of the individual CK2 subunits observed in living cells is crucial in the control of the many cellular processes that are governed by this pleiotropic kinase. Indeed, previous studies reported that the unbalanced expression of CK2 subunits is sufficient to drive epithelial to mesenchymal transition (EMT), a process involved in cancer invasion and metastasis. Moreover, sub-stoichiometric expression of CK2β compared to CK2α in a subset of breast cancer tumors was correlated with the induction of EMT markers and increased epithelial cell plasticity in breast carcinoma progression. Phenotypic changes of epithelial cells are often associated with the activation of phosphotyrosine signaling. Herein, using phosphotyrosine enrichment coupled with affinity capture and proteomic analysis, we show that decreased expression of CK2β in MCF10A mammary epithelial cells triggers the phosphorylation of a number of proteins on tyrosine residues and promotes the striking activation of the FAK1-Src-PAX1 signaling pathway. Moreover, morphometric analyses also reveal that CK2β loss increases the number and the spatial distribution of focal adhesion signaling complexes that coordinate the adhesive and migratory processes. Together, our findings allow positioning CK2β as a gatekeeper for cell spreading by restraining focal adhesion formation and invasion of mammary epithelial cells.
Language	English
Publishing date	2022-06-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2022.900947
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Article ; Online: Differential bioactivity of four BMP-family members as function of biomaterial stiffness.

Sales, Adrià / Khodr, Valia / Machillot, Paul / Chaar, Line / Fourel, Laure / Guevara-Garcia, Amaris / Migliorini, Elisa / Albigès-Rizo, Corinne / Picart, Catherine

Biomaterials

2022 Volume 281, Page(s) 121363

Abstract: While a soft film itself is not able to induce cell spreading, BMP-2 presented via such soft film (so called "matrix-bound BMP-2") was previously shown to trigger cell spreading, migration and downstream BMP-2 signaling. Here, we used thin films of ... ...

Abstract	While a soft film itself is not able to induce cell spreading, BMP-2 presented via such soft film (so called "matrix-bound BMP-2") was previously shown to trigger cell spreading, migration and downstream BMP-2 signaling. Here, we used thin films of controlled stiffness presenting matrix-bound BMPs to study the effect of four BMP members (BMP-2, 4, 7, 9) on cell adhesion and differentiation of skeletal progenitors. We performed automated high-content screening of cellular responses, including cell number, cell spreading area, SMAD phosphorylation and alkaline phosphatase activity. We revealed that the cell response to bBMPs is BMP-type specific, and involved certain BMP receptors and beta chain integrins. In addition, this response is stiffness-dependent for several receptors. The basolateral presentation of the BMPs allowed us to discriminate the specificity of cellular response, especiallyd the role of type I and II BMP receptors and of β integrins in a BMP-type and stiffness-dependent manner. Notably, BMP-2 and BMP-4 were found to have distinct roles, while ALK5, previously known as a TGF-β receptor was revealed to be involved in the BMP-pathway.
MeSH term(s)	Biocompatible Materials ; Bone Morphogenetic Protein Receptors/metabolism ; Bone Morphogenetic Proteins/metabolism ; Cell Differentiation ; Signal Transduction/physiology ; Smad Proteins/metabolism ; Transforming Growth Factor beta/metabolism
Chemical Substances	Biocompatible Materials ; Bone Morphogenetic Proteins ; Smad Proteins ; Transforming Growth Factor beta ; Bone Morphogenetic Protein Receptors (EC 2.7.11.30)
Language	English
Publishing date	2022-01-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603079-8
ISSN	1878-5905 ; 0142-9612
ISSN (online)	1878-5905
ISSN	0142-9612
DOI	10.1016/j.biomaterials.2022.121363
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Article: Interplay between integrins and cadherins to control bone differentiation upon BMP-2 stimulation.

Valat, Anne / Fourel, Laure / Sales, Adria / Machillot, Paul / Bouin, Anne-Pascale / Fournier, Carole / Bosc, Lauriane / Arboléas, Mélanie / Bourrin-Reynard, Ingrid / Wagoner Johnson, Amy J / Bruckert, Franz / Albigès-Rizo, Corinne / Picart, Catherine

Frontiers in cell and developmental biology

2023 Volume 10, Page(s) 1027334

Abstract: Introduction: ...

Abstract	Introduction:
Language	English
Publishing date	2023-01-04
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2022.1027334
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Article ; Online: Learning from BMPs and their biophysical extracellular matrix microenvironment for biomaterial design.

Migliorini, Elisa / Guevara-Garcia, Amaris / Albiges-Rizo, Corinne / Picart, Catherine

Bone

2020 Volume 141, Page(s) 115540

Abstract: It is nowadays well-accepted that the extracellular matrix (ECM) is not a simple reservoir for growth factors but is an organization center of their biological activity. In this review, we focus on the ability of the ECM to regulate the biological ... ...

Abstract	It is nowadays well-accepted that the extracellular matrix (ECM) is not a simple reservoir for growth factors but is an organization center of their biological activity. In this review, we focus on the ability of the ECM to regulate the biological activity of BMPs. In particular, we survey the role of the ECM components, notably the glycosaminoglycans and fibrillary ECM proteins, which can be promoters or repressors of the biological activities mediated by the BMPs. We examine how a process called mechano-transduction induced by the ECM can affect BMP signaling, including BMP internalization by the cells. We also focus on the spatio-temporal regulation of the BMPs, including their release from the ECM, which enables to modulate their spatial localization as well as their local concentration. We highlight how biomaterials can recapitulate some aspects of the BMPs/ECM interactions and help to answer fundamental questions to reveal previously unknown molecular mechanisms. Finally, the design of new biomaterials inspired by the ECM to better present BMPs is discussed, and their use for a more efficient bone regeneration in vivo is also highlighted.
MeSH term(s)	Animals ; Biocompatible Materials ; Bone Morphogenetic Proteins ; Extracellular Matrix ; Extracellular Matrix Proteins ; Humans ; Signal Transduction
Chemical Substances	Biocompatible Materials ; Bone Morphogenetic Proteins ; Extracellular Matrix Proteins
Language	English
Publishing date	2020-07-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	632515-4
ISSN	1873-2763 ; 8756-3282
ISSN (online)	1873-2763
ISSN	8756-3282
DOI	10.1016/j.bone.2020.115540
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Zs.A 1571: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 332: Show issues

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Article ; Online: Calcium signaling mediates a biphasic mechanoadaptive response of endothelial cells to cyclic mechanical stretch.

Miroshnikova, Yekaterina A / Manet, Sandra / Li, Xinping / Wickström, Sara A / Faurobert, Eva / Albiges-Rizo, Corinne

Molecular biology of the cell

2021 Volume 32, Issue 18, Page(s) 1724–1736

Abstract: The vascular system is precisely regulated to adjust blood flow to organismal demand, thereby guaranteeing adequate perfusion under varying physiological conditions. Mechanical forces, such as cyclic circumferential stretch, are among the critical ... ...

Abstract	The vascular system is precisely regulated to adjust blood flow to organismal demand, thereby guaranteeing adequate perfusion under varying physiological conditions. Mechanical forces, such as cyclic circumferential stretch, are among the critical stimuli that dynamically adjust vessel distribution and diameter, but the precise mechanisms of adaptation to changing forces are unclear. We find that endothelial monolayers respond to cyclic stretch by transient remodeling of the vascular endothelial cadherin-based adherens junctions and the associated actomyosin cytoskeleton. Time-resolved proteomic profiling reveals that this remodeling is driven by calcium influx through the mechanosensitive Piezo1 channel, triggering Rho activation to increase actomyosin contraction. As the mechanical stimulus persists, calcium signaling is attenuated through transient down-regulation of Piezo1 protein. At the same time, filamins are phosphorylated to increase monolayer stiffness, allowing mechanoadaptation to restore junctional integrity despite continuing exposure to stretch. Collectively, this study identifies a biphasic response to cyclic stretch, consisting of an initial calcium-driven junctional mechanoresponse, followed by mechanoadaptation facilitated by monolayer stiffening.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actomyosin/metabolism ; Adherens Junctions/physiology ; Antigens, CD/genetics ; Antigens, CD/metabolism ; Biomechanical Phenomena ; Cadherins/genetics ; Cadherins/metabolism ; Calcimycin/pharmacology ; Calcium Ionophores/pharmacology ; Calcium Signaling/drug effects ; Cytochalasin D/pharmacology ; Filamins/metabolism ; Human Umbilical Vein Endothelial Cells ; Humans ; Ion Channels/genetics ; Ion Channels/metabolism ; Mechanotransduction, Cellular ; Phosphoproteins/analysis ; Phosphoproteins/metabolism ; Protein Interaction Maps ; p21-Activated Kinases/metabolism ; rac GTP-Binding Proteins/metabolism ; rhoA GTP-Binding Protein/metabolism
Chemical Substances	Antigens, CD ; Cadherins ; Calcium Ionophores ; Filamins ; Ion Channels ; PIEZO1 protein, human ; Phosphoproteins ; cadherin 5 ; RHOA protein, human (124671-05-2) ; Cytochalasin D (22144-77-0) ; Calcimycin (37H9VM9WZL) ; Actomyosin (9013-26-7) ; PAK1 protein, human (EC 2.7.11.1) ; p21-Activated Kinases (EC 2.7.11.1) ; rac GTP-Binding Proteins (EC 3.6.5.2) ; rhoA GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2021-06-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E21-03-0106
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 410: Show issues

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Article ; Online: CK2β Is a Gatekeeper of Focal Adhesions Regulating Cell Spreading

Odile Filhol / Anne-Marie Hesse / Anne-Pascale Bouin / Corinne Albigès-Rizo / Florian Jeanneret / Christophe Battail / Delphine Pflieger / Claude Cochet

Frontiers in Molecular Biosciences, Vol

2022 Volume 9

Abstract: CK2 is a hetero-tetrameric serine/threonine protein kinase made up of two CK2α/αʹ catalytic subunits and two CK2β regulatory subunits. The free CK2α subunit and the tetrameric holoenzyme have distinct substrate specificity profiles, suggesting that the ... ...

Abstract	CK2 is a hetero-tetrameric serine/threonine protein kinase made up of two CK2α/αʹ catalytic subunits and two CK2β regulatory subunits. The free CK2α subunit and the tetrameric holoenzyme have distinct substrate specificity profiles, suggesting that the spatiotemporal organization of the individual CK2 subunits observed in living cells is crucial in the control of the many cellular processes that are governed by this pleiotropic kinase. Indeed, previous studies reported that the unbalanced expression of CK2 subunits is sufficient to drive epithelial to mesenchymal transition (EMT), a process involved in cancer invasion and metastasis. Moreover, sub-stoichiometric expression of CK2β compared to CK2α in a subset of breast cancer tumors was correlated with the induction of EMT markers and increased epithelial cell plasticity in breast carcinoma progression. Phenotypic changes of epithelial cells are often associated with the activation of phosphotyrosine signaling. Herein, using phosphotyrosine enrichment coupled with affinity capture and proteomic analysis, we show that decreased expression of CK2β in MCF10A mammary epithelial cells triggers the phosphorylation of a number of proteins on tyrosine residues and promotes the striking activation of the FAK1-Src-PAX1 signaling pathway. Moreover, morphometric analyses also reveal that CK2β loss increases the number and the spatial distribution of focal adhesion signaling complexes that coordinate the adhesive and migratory processes. Together, our findings allow positioning CK2β as a gatekeeper for cell spreading by restraining focal adhesion formation and invasion of mammary epithelial cells.
Keywords	CK2β depletion ; EMT ; tyrosine-phosphorylated proteins ; FAK1-Src-PAX1 signaling pathway ; focal adhesions ; epithelial cell spreading ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2022-06-01T00:00:00Z
Publisher	Frontiers Media S.A.
Document type	Article ; Online
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Article ; Online: QuanTI-FRET: a framework for quantitative FRET measurements in living cells.

Coullomb, Alexis / Bidan, Cécile M / Qian, Chen / Wehnekamp, Fabian / Oddou, Christiane / Albigès-Rizo, Corinne / Lamb, Don C / Dupont, Aurélie

Scientific reports

2020 Volume 10, Issue 1, Page(s) 6504

Abstract: Förster Resonance Energy Transfer (FRET) allows for the visualization of nanometer-scale distances and distance changes. This sensitivity is regularly achieved in single-molecule experiments in vitro but is still challenging in biological materials. ... ...

Abstract	Förster Resonance Energy Transfer (FRET) allows for the visualization of nanometer-scale distances and distance changes. This sensitivity is regularly achieved in single-molecule experiments in vitro but is still challenging in biological materials. Despite many efforts, quantitative FRET in living samples is either restricted to specific instruments or limited by the complexity of the required analysis. With the recent development and expanding utilization of FRET-based biosensors, it becomes essential to allow biologists to produce quantitative results that can directly be compared. Here, we present a new calibration and analysis method allowing for quantitative FRET imaging in living cells with a simple fluorescence microscope. Aside from the spectral crosstalk corrections, two additional correction factors were defined from photophysical equations, describing the relative differences in excitation and detection efficiencies. The calibration is achieved in a single step, which renders the Quantitative Three-Image FRET (QuanTI-FRET) method extremely robust. The only requirement is a sample of known stoichiometry donor:acceptor, which is naturally the case for intramolecular FRET constructs. We show that QuanTI-FRET gives absolute FRET values, independent of the instrument or the expression level. Through the calculation of the stoichiometry, we assess the quality of the data thus making QuanTI-FRET usable confidently by non-specialists.
MeSH term(s)	Biosensing Techniques ; Evaluation Studies as Topic ; Fluorescence ; Fluorescence Resonance Energy Transfer/methods
Language	English
Publishing date	2020-04-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-62924-w
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Article ; Online: Mechanotransduction pulls the strings of matrix degradation at invadosome.

Mrkonjic, Sanela / Destaing, Olivier / Albiges-Rizo, Corinne

Matrix biology : journal of the International Society for Matrix Biology

2017 Volume 57-58, Page(s) 190–203

Abstract: Degradation of the extracellular matrix is a critical step of tumor cell invasion. Both protease-dependent and -independent mechanisms have been described as alternate processes in cancer cell motility. Interestingly, some effectors of protease-dependent ...

Abstract	Degradation of the extracellular matrix is a critical step of tumor cell invasion. Both protease-dependent and -independent mechanisms have been described as alternate processes in cancer cell motility. Interestingly, some effectors of protease-dependent degradation are focalized at invadosomes and are directly coupled with contractile and adhesive machineries composed of multiple mechanosensitive proteins. This review presents recent findings in protease-dependent mechanisms elucidating the ways the force affects extracellular matrix degradation by targeting protease expression and activity at invadosome. The aim is to highlight mechanosensing and mechanotransduction processes to direct the degradative activity at invadosomes, with the focus on membrane tension, proteases and mechanosensitive ion channels.
Language	English
Publishing date	2017-01
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	1183793-7
ISSN	1569-1802 ; 0945-053X
ISSN (online)	1569-1802
ISSN	0945-053X
DOI	10.1016/j.matbio.2016.06.007
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Zs.A 1694: Show issues

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Article ; Online: Immunofluorescence of Cell-Cell and Cell-Extracellular Matrix Adhesive Defects in In Vitro Endothelial CCM Model: Juxtacrine Role of Mutant Extracellular Matrix on Wild-Type Endothelial Cells.

Manet, Sandra / Vannier, Daphné / Bouin, Anne-Pascale / Lisowska, Justyna / Albiges-Rizo, Corinne / Faurobert, Eva

Methods in molecular biology (Clifton, N.J.)

2020 Volume 2152, Page(s) 401–416

Abstract: Endothelial cells lining cerebral cavernous malformations (CCM) present strong adhesive and mechanical defects. Increased cell contractility is a driver to the onset and the expansion of the CCM lesions. 2D in vitro endothelial models have been developed ...

Abstract	Endothelial cells lining cerebral cavernous malformations (CCM) present strong adhesive and mechanical defects. Increased cell contractility is a driver to the onset and the expansion of the CCM lesions. 2D in vitro endothelial models have been developed from either endothelial cells isolated from ccm1-3 knock-out mice or CCM1-3-silenced primary endothelial cells. These in vitro models faithfully recapitulate the adhesive and contractile defects of the CCM-deficient endothelial cells such as increased cell-extracellular matrix (ECM) adhesion through β1 integrin-anchored actin stress fibers, abnormal remodeling of the ECM, and destabilized VE-cadherin-dependent cell-cell junctions. Using such 2D in vitro CCM models, we have shown that the ECM remodeled by CCM-depleted endothelial cells can propagate CCM-like adhesive defects to wild-type endothelial cells, a process potentially pertinent to CCM lesion expansion. Here, we detail methods for studying the morphology of focal adhesions, actomyosin cytoskeleton, and VE-cadherin-dependent Adherens junctions by immunofluorescence and morphometric analyses. Moreover, we detail the protocols to produce and purify remodeled ECM and to test its effect on endothelial cell adhesion.
MeSH term(s)	Adherens Junctions/metabolism ; Animals ; Biomarkers ; Cell Adhesion ; Cell Communication ; Cytoskeleton/metabolism ; Endothelial Cells/metabolism ; Endothelium, Vascular/metabolism ; Extracellular Matrix/metabolism ; Fluorescent Antibody Technique ; Focal Adhesions/metabolism ; Hemangioma, Cavernous, Central Nervous System/etiology ; Hemangioma, Cavernous, Central Nervous System/metabolism ; Hemangioma, Cavernous, Central Nervous System/pathology ; Human Umbilical Vein Endothelial Cells ; Humans ; Intercellular Junctions/metabolism ; Mechanotransduction, Cellular ; Models, Biological
Chemical Substances	Biomarkers
Language	English
Publishing date	2020-06-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-0640-7_29
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