TY - JOUR
T1 - Syndecans, signaling, and cell adhesion.
AU - Couchman, J R
AU - Woods, A
N1 - Keywords: Amino Acid Sequence; Animals; Cell Adhesion; Extracellular Matrix; Membrane Glycoproteins; Molecular Sequence Data; Proteoglycans; Signal Transduction; Syndecans
PY - 1996
Y1 - 1996
N2 - Syndecans are transmembrane proteoglycans which can participate in diverse cell surface interactions, involving extracellular matrix macromolecules, growth factors, protease inhibitors, and even viral entry. Currently, all extracellular interactions are believed to be mediated by distinct structures within the heparan sulfate chains, leaving the roles of chondroitin sulfate chains and extracellular portion of the core proteins to be elucidated. Evidence that syndecans are a class of receptor involved in cell adhesion is mounting, and their small cytoplasmic domains may link with the microfilament cytoskeleton, thereby mediating signaling events. The molecular details are unknown, but the conservation of regions of syndecan cytoplasmic domains, and a strong tendency for homotypic association, support the idea that the ligand-induced clustering may be a discrete source of specific transmembrane signaling from matrix to cytoskeleton, as proposed for other classes of adhesion receptors.
AB - Syndecans are transmembrane proteoglycans which can participate in diverse cell surface interactions, involving extracellular matrix macromolecules, growth factors, protease inhibitors, and even viral entry. Currently, all extracellular interactions are believed to be mediated by distinct structures within the heparan sulfate chains, leaving the roles of chondroitin sulfate chains and extracellular portion of the core proteins to be elucidated. Evidence that syndecans are a class of receptor involved in cell adhesion is mounting, and their small cytoplasmic domains may link with the microfilament cytoskeleton, thereby mediating signaling events. The molecular details are unknown, but the conservation of regions of syndecan cytoplasmic domains, and a strong tendency for homotypic association, support the idea that the ligand-induced clustering may be a discrete source of specific transmembrane signaling from matrix to cytoskeleton, as proposed for other classes of adhesion receptors.
U2 - 10.1002/(SICI)1097-4644(19960616)61:4<578::AID-JCB11>3.0.CO;2-C
DO - 10.1002/(SICI)1097-4644(19960616)61:4<578::AID-JCB11>3.0.CO;2-C
M3 - Journal article
C2 - 8806081
SN - 0730-2312
VL - 61
SP - 578
EP - 584
JO - Journal of Cellular Biochemistry
JF - Journal of Cellular Biochemistry
IS - 4
ER -