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
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