VE-cadherin-induced Cdc42 signaling regulates formation of membrane protrusions in endothelial cells
| dc.contributor.author | Kouklis, P. | en |
| dc.contributor.author | Konstantoulaki, M. | en |
| dc.contributor.author | Malik, A. B. | en |
| dc.date.accessioned | 2015-11-24T18:50:55Z | |
| dc.date.available | 2015-11-24T18:50:55Z | |
| dc.identifier.issn | 0021-9258 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/18177 | |
| dc.rights | Default Licence | - |
| dc.subject | Antigens, CD | en |
| dc.subject | Cadherins/*physiology | en |
| dc.subject | Catenins | en |
| dc.subject | Cell Adhesion Molecules/physiology | en |
| dc.subject | Cell Membrane/*metabolism | en |
| dc.subject | Cells, Cultured | en |
| dc.subject | Cytoskeletal Proteins/physiology | en |
| dc.subject | Endothelium, Vascular/*cytology/ultrastructure | en |
| dc.subject | Humans | en |
| dc.subject | Phosphoproteins/physiology | en |
| dc.subject | Trans-Activators/physiology | en |
| dc.subject | beta Catenin | en |
| dc.subject | cdc42 GTP-Binding Protein/*physiology | en |
| dc.title | VE-cadherin-induced Cdc42 signaling regulates formation of membrane protrusions in endothelial cells | en |
| heal.abstract | The cytoplasmic domain of cadherins and the associated catenins link the cytoskeleton with signal transduction pathways. To study the signaling function of non-junctional VE-cadherin, which can form during the loss VE-cadherin homotypic adhesion, wild type VE-cadherin or VE-cadherin cytoplasmic domain (DeltaEXD) was expressed in sub-confluent endothelial cells. We observed that Cdc42 was activated in transfected cells and that these cells also developed Cdc42-dependent >70-microm-long plasma membrane protrusions. The formation of these structures required actin polymerization, and they developed specifically in endothelial cells as compared with epithelial cells. Expression of the VE-cadherin cytoplasmic domain lacking the beta-catenin binding site also induced Cdc42 activation; thus, its activation cannot be ascribed to beta-catenin binding. However, these cells were not able to form the protrusions. These results suggest that the cytoplasmic domain of non-junctional VE-cadherin can serve as a scaffold involved in Cdc42 activation at the endothelial plasma membrane. beta-Catenin and the associated alpha-catenin may serve as support sites for actin polymerization, leading to formation of long plasma membrane protrusions. Thus, non-junctional VE-cadherin actively participates in inside-out signaling at the plasma membrane, leading to the development of endothelial membrane protrusions. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | 10.1074/jbc.M212591200 | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/12595527 | - |
| heal.identifier.secondary | http://www.jbc.org/content/278/18/16230.full.pdf | - |
| heal.journalName | J Biol Chem | en |
| heal.journalType | peer-reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2003 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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