Structure of artificial and natural VE-cadherinbased adherens junctions
Autor: | Jean-Christophe Taveau, Sébastien Almagro, Elizabeth A. Hewat, Stéphanie Heyraud, Mathilde Dubois, Claire Durmort, Olivier Lambert, Danielle Gulino-Debrac, Olivier Le Bihan, Sylvain Trépout |
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Přispěvatelé: | UMR UJF-CEA(IRTSV)-INSERM U882 Laboratoire d'angiogenèse et physiopathologie vasculaire (LAPV U882), Chimie et Biologie des Membranes et des Nanoobjets (CBMN), Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie vasculaire : interactions cellulaires, signalisation et vieillissement, 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), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-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)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-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), Gulino-Debrac, Danielle |
Rok vydání: | 2008 |
Předmět: |
Models
Molecular [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology endothelial junction MESH: Actins Biochemistry Article MESH: Cadherins MESH: Cell Adhesion Adherens junction 03 medical and health sciences 0302 clinical medicine Cell–cell interaction Cryoelectron microscopy annexin 2 [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology Cell Adhesion Animals Humans MESH: Animals [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology 3D reconstruction VE cadherin 030304 developmental biology 0303 health sciences MESH: Humans Cadherin Membranes Artificial Adherens Junctions Cadherins Actin cytoskeleton Actins Cell biology Endothelial stem cell MESH: Adherens Junctions 030220 oncology & carcinogenesis Catenin Endothelium Vascular MESH: Cryoelectron Microscopy MESH: Endothelium Vascular MESH: Membranes Artificial VE-cadherin MESH: Models Molecular Annexin A2 |
Zdroj: | Biochemical Society Transactions Biochemical Society Transactions, Portland Press, 2008, 36 (2), pp.189-193. ⟨10.1042/BST0360189⟩ Biochemical Society Transactions, Portland Press, 2008, 36 (Pt 2), pp.189-93. ⟨10.1042/BST0360189⟩ Biochemical Society Transactions, 2008, 36 (Pt 2), pp.189-93. ⟨10.1042/BST0360189⟩ |
ISSN: | 1470-8752 0300-5127 |
DOI: | 10.1042/bst0360189 |
Popis: | International audience; In vascular endothelium, adherens junctions between endothelial cells are composed of VE-cadherin (vascular endothelial cadherin), an adhesive receptor that is crucial for the proper assembly of vascular structures and the maintenance of vascular integrity. As a classical cadherin, VE-cadherin links endothelial cells together by homophilic interactions mediated by its extracellular part and associates intracellularly with the actin cytoskeleton via catenins. Although, from structural crystallographic data, a dimeric structure arranged in a trans orientation has emerged as a potential mechanism of cell-cell adhesion, the cadherin organization within adherens junctions remains controversial. Concerning VE-cadherin, its extracellular part possesses the capacity to self-associate in solution as hexamers consisting of three antiparallel cadherin dimers. VE-cadherin-based adherens junctions were reconstituted in vitro by assembly of a VE-cadherin EC (extracellular repeat) 1-EC4 hexamer at the surfaces of liposomes. The artificial adherens junctions revealed by cryoelectron microscopy appear as a two-dimensional self-assembly of hexameric structures. This cadherin organization is reminiscent of that found in native desmosomal junctions. Further structural studies performed on native VE-cadherin junctions would provide a better understanding of the cadherin organization within adherens junctions. Homophilic interactions between cadherins are strengthened intracellularly by connection to the actin cytoskeleton. Recently, we have discovered that annexin 2, an actin-binding protein connects the VE-cadherin-catenin complex to the actin cytoskeleton. This novel link is labile and promotes the endothelial cell switch from a quiescent to an angiogenic state. |
Databáze: | OpenAIRE |
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