Abstract
The vertebrate syndecans, which make up a four-member family of small type I transmembrane heparan sulfate proteoglycans, constitute evolutionarily conserved family proteins. In particular, sequences in the transmembrane and cytoplasmic domains are a unifying feature within the family. However, the extracellular domain sequences are molecule-specific, implying that different syndecans have evolved to carry out similar, but non-identical, functions. While all four syndecans have been implicated in regulation of the cytoskeleton, their roles are clearly complex. Recent developments indicate that the closely related syndecan-2 and -4 have separable functions, though both bind a number of ligands through their heparan sulfate chains. The specification of these activities is probably core protein related, but is it due to a distinct expression pattern or molecule-specific regulatory mechanisms? Although there is not yet enough data to provide unambiguous answers, here we shall review the known functions and regulatory mechanisms of syndecan-2 and -4.
Original language | English |
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Pages (from-to) | 181-187 |
Number of pages | 7 |
Journal | Molecules and Cells |
Volume | 17 |
Issue number | 2 |
DOIs | |
State | Published - 30 Apr 2004 |
Keywords
- Cell adhesion
- Cytoskeleton
- Extracellular matrix
- Signal transduction
- Syndecans