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Details on Person Syndecans are type I transmembrane proteins, with an N-termi...
| Class:Id | Summation:2731111 |
|---|---|
| _displayName | Syndecans are type I transmembrane proteins, with an N-termi... |
| _timestamp | 2012-12-19 17:27:53 |
| created | [InstanceEdit:2731117] Jupe, S, 2012-12-05 |
| literatureReference | [LiteratureReference:2682306] Transmembrane domain-induced oligomerization is crucial for the functions of syndecan-2 and syndecan-4 [LiteratureReference:2681684] Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region [LiteratureReference:2682218] Function of the syndecan-4 cytoplasmic domain in oligomerization and association with ?-actinin in turkey muscle satellite cells [LiteratureReference:2682229] Syndecans in wound healing, inflammation and vascular biology [LiteratureReference:2684466] Ligand-affinity cloning and structure of a cell surface heparan sulfate proteoglycan that binds basic fibroblast growth factor [LiteratureReference:2684492] Possible regulation of FGF activity by syndecan, an integral membrane heparan sulfate proteoglycan [LiteratureReference:2682290] Stimulation of fibroblast growth factor receptor-1 occupancy and signaling by cell surface-associated syndecans and glypican [LiteratureReference:2684493] Syndecan-2 regulates transforming growth factor-beta signaling [LiteratureReference:2684476] Syndecan-4 as a molecule involved in defense mechanisms [LiteratureReference:2682240] Syndecans: new kids on the signaling block [LiteratureReference:2684477] Heparan sulfate-mediated binding of epithelial cell surface proteoglycan to thrombospondin [LiteratureReference:2731083] Syndecan-1 mediates cell spreading in transfected human lymphoblastoid (Raji) cells [LiteratureReference:2682305] Regulation of cytoskeletal organization by syndecan transmembrane proteoglycans [LiteratureReference:2682228] Delayed wound repair and impaired angiogenesis in mice lacking syndecan-4 [LiteratureReference:2682312] Syndecan-4 deficiency leads to high mortality of lipopolysaccharide-injected mice [LiteratureReference:2682286] Role of syndecan-1 in leukocyte-endothelial interactions in the ocular vasculature |
| modified | [InstanceEdit:2867920] Jupe, S, 2012-12-19 |
| text | Syndecans are type I transmembrane proteins, with an N-terminal ectodomain that contains several consensus sequences for glycosaminoglycan (GAG) attachment and a short C-terminal cytoplasmic domain. Syndecan-1 and -3 GAG attachment sites occur in two distinct clusters, one near the N-terminus and the other near the membrane-attachment site, separated by a proline and threonine-rich 'spacer'. Syndecan ectodomain sequences are poorly conserved in the family and between species, but the transmembrane and cytoplasmic domains are highly conserved. Syndecan-1 and -3 form a subfamily. Syndecan core proteins form dimers (Choi et al. 2007) and at least syndecan-3 and -4 form oligomers (Asundi & Carey 1995, Shin et al. 2012). Syndecan-1 is the major syndecan of epithelial cells including vascular endothelium. Syndecan-2 is present mostly in mesenchymal, neuronal and smooth muscle cells, syndecan-3 is the major syndecan of the nervous system , while syndecan-4 is ubiquitously expressed but at lower levels than the other syndecans (refs in Alexopoulou et al. 2007). Syndecans have attached heparan sulfate (HS) and to a lesser extent chondroitin sulfate (CS) chains. These allow interactions with a large number of proteins, including heparin-binding growth factors such as fibroblast growth factors (Kiefer et al. 1990, Bernfield & Hooper 1991, Steinfeld et al. 1996), vascular endothelial growth factors (VEGFs) and transforming growth factor-Beta (Chen et al. 2000, Ishiguro et al. 2002). Various enzymes involved in post-translational HS chain modifications produce unique binding motifs that selectively recognize different proteins (Tkachenko et al. 2005). HS chains facilitate interactions of syndecan-1 with extracellular matrix proteins, including thrombospondin-1 (Sun et al. 1989, Lebakken & Rapraeger 1996, Yoneda & Couchman 2003). Syndecan-null mice have subtle phenotypes when compared with mice deficient in HS chain synthesis or modification (Echtermeyer et al. 2001, Ishiquro et al. 2001, Götte et al. 2002). GPI-anchored glypicans and matrix HSPGs such as perlecan may compensate for the absence of syndecans. |
| (summation) | [Reaction:2731112] Syndecan-1 binds THBS1 [Homo sapiens] |
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