PUBLICATION
Structural and cell adhesion properties of zebrafish syndecan-4 are shared with higher vertebrates
- Authors
- Whiteford, J.R., Ko, S., Lee, W., and Couchman, J.R.
- ID
- ZDB-PUB-080902-19
- Date
- 2008
- Source
- The Journal of biological chemistry 283(43): 29322-29330 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Motifs
- Amino Acid Sequence
- Animals
- Base Sequence
- CHO Cells
- Cell Adhesion
- Cricetinae
- Cricetulus
- Dimerization
- Mice
- Molecular Sequence Data
- Phosphatidylinositol 4,5-Diphosphate/chemistry
- Rats
- Syndecan-4/chemistry*
- Syndecan-4/physiology*
- Zebrafish
- PubMed
- 18753130 Full text @ J. Biol. Chem.
Citation
Whiteford, J.R., Ko, S., Lee, W., and Couchman, J.R. (2008) Structural and cell adhesion properties of zebrafish syndecan-4 are shared with higher vertebrates. The Journal of biological chemistry. 283(43):29322-29330.
Abstract
The syndecan proteoglycans are an ancient class of receptor, bearing heparan sulfate chains that interact with numerous potential ligands including growth factors, morphogens and extracellular matrix molecules.The single syndecan of invertebrates appears not to have cell adhesion roles, but these have been described for mammalian paralogues, especially syndecan-4. This member is best understood in terms of interactions, signaling and structure of its cytoplasmic domain. The zebrafish homologue of syndecan-4 has been genetically linked to cell adhesion and migration in zebrafish embryos, but no molecular and cellular studies have been reported. Here it is demonstrated that key functional attributes of syndecan-4 are common to both zebrafish and mammalian homologues. These include glycosaminoglycan substitution, a NXIP motif in the extracellular domain that promotes integrin-mediated cell adhesion, and a transmembrane GXXXG motif that promotes dimer formation. In addition, despite some amino acid substitutions in the cytoplasmic domain, its ability to form twisted clamp dimers is preserved, as revealed by nuclear magnetic resonance spectroscopy. This technique also showed that phosphatidylinositol 4,5 bisphosphate can interact with the zebrafish syndecan-4 cytoplasmic domain, and that the molecule in its entirety supports focal adhesion formation, and complements the murine null cells to restore a normal actin cytoskeleton identically to the rat homologue. Therefore, the cell adhesion properties of syndecan-4 are consistent across the vertebrate spectrum and reflect an early acquisition of specialisation after syndecan gene duplication events at the invertebrate/early chordate boundary.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping