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

VL - 61

SP - 578

EP - 584

JO - Journal of cellular biochemistry. Supplement

JF - Journal of cellular biochemistry. Supplement

SN - 0733-1959

IS - 4

ER -