Syndesmos, a Syndecan-4 Cytoplasmic Domain Interactor, Binds to the Focal Adhesion Adaptor Proteins Paxillin and Hic-5
Autor: | Paul F. Goetinck, Becki French, Stefania Saoncella, So-Hyung Lee, Wendy Neveu, Fabienne Denhez, Peter C. Baciu, Sarah A. Wilcox-Adelman |
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Rok vydání: | 2002 |
Předmět: |
animal structures
Transcription Genetic Recombinant Fusion Proteins Molecular Sequence Data PTK2 Integrin Chick Embryo macromolecular substances Models Biological environment and public health Biochemistry Syndecan 1 Focal adhesion Cell Adhesion Animals Amino Acid Sequence Protein kinase A Molecular Biology Cells Cultured Protein Kinase C Paxillin Actin Glutathione Transferase Sequence Homology Amino Acid biology Chemistry Intracellular Signaling Peptides and Proteins Signal transducing adaptor protein Cell Biology LIM Domain Proteins Phosphoproteins Precipitin Tests Actins Protein Structure Tertiary Cell biology DNA-Binding Proteins Cytoskeletal Proteins Protein Biosynthesis biology.protein biological phenomena cell phenomena and immunity Carrier Proteins Protein Binding Signal Transduction |
Zdroj: | Journal of Biological Chemistry. 277:12270-12274 |
ISSN: | 0021-9258 |
Popis: | Syndecan-4 and integrins are the primary transmembrane receptors of focal adhesions in cells adherent to extracellular matrix molecules. Syndesmos is a cytoplasmic protein that interacts specifically with the cytoplasmic domain of syndecan-4, and it co-localizes with syndecan-4 in focal contacts. In the present study we sought possible interactors with syndesmos. We find that syndesmos interacts with the focal adhesion adaptor protein paxillin. The binding of syndesmos to paxillin is direct, and these interactions are triggered by the activation of protein kinase C. Syndesmos also binds the paxillin homolog, Hic-5. The connection of syndecan-4 with paxillin through syndesmos parallels the connection between paxillin and integrins and may thus reflect the cooperative signaling of these two receptors in the assembly of focal adhesions and actin stress fibers. |
Databáze: | OpenAIRE |
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