PUBLICATION
A conserved NXIP motif is required for cell adhesion properties of the syndecan-4 ectodomain
- Authors
- Whiteford, J.R., and Couchman, J.R.
- ID
- ZDB-PUB-060906-8
- Date
- 2006
- Source
- The Journal of biological chemistry 281(43): 32156-32163 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Conserved Sequence
- Amino Acid Motifs
- Dogs
- Skin/cytology
- Chlorocebus aethiops
- PubMed
- 16936286 Full text @ J. Biol. Chem.
Abstract
Syndecans are cell surface proteoglycans involved in cell adhesion and motility. Syndecan-4 is an important component of focal adhesions and is involved in cytoskeletal reorganisation. Previous work has shown that the syndecan-4 ectodomain can support cell attachment. Here, three vertebrate syndecan-4 ectodomains are compared including that of the zebrafish and we demonstrate that the cell binding activity of the syndecan-4 ectodomain is conserved. Cell adhesion to the syndecan-4 ectodomain appears to be a characteristic of mesenchymal cells. Comparison of syndecan-4 ectodomain sequences lead to the identification of three conserved regions of sequence of which one, an NXIP motif, is important for cell binding activity. We show that cell adhesion to the syndecan-4 ectodomain involves ss1 integrins in several cell types.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping