Cytoskeleton assembly at endothelial cell-cell contacts is regulated by alphaII-spectrin-VASP complexes.

Journal article

Directed cortical actin assembly is the driving force for intercellular adhesion. Regulated by phosphorylation, vasodilator-stimulated phosphoprotein (VASP) participates in actin fiber formation. We screened for endothelial proteins, which bind to VASP, dependent on its phosphorylation status. Differential proteomics identified alphaII-spectrin as such a VASP-interacting protein. alphaII-Spectrin binds to the VASP triple GP(5)-motif via its SH3 domain. cAMP-dependent protein kinase-mediated V...

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Authors: Benz, P; Blume, C; Moebius, J; Oschatz, C; Schuh, K

• Publication status: Published
• Journal: Journal of cell biology
• Volume: 180
• Issue: 1
• Pages: 205-219
• Publication date: 2008-01-01
• DOI: 10.1083/jcb.200709181
• EISSN: 1540-8140
• ISSN: 0021-9525
• Language: English
• Keywords: Amino Acid Sequence; Animals; Binding Sites; Intercellular Junctions; Protein Interaction Domains and Motifs; Phosphorylation; Mice; Cell Adhesion Molecules; Cell Adhesion; Carrier Proteins; Protein Interaction Mapping; Endothelial Cells; Actin Cytoskeleton; Microfilament Proteins; Molecular Sequence Data; Phosphoproteins