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Details on Person Syndecans have attached heparan sulfate (HS) and to a lesser...

Class:IdSummation:2750178
_displayNameSyndecans have attached heparan sulfate (HS) and to a lesser...
_timestamp2013-05-22 10:38:57
created[InstanceEdit:2750182] Jupe, S, 2012-12-06
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:2682240] Syndecans: new kids on the signaling block
[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
[LiteratureReference:2682272] Synbindin, A novel syndecan-2-binding protein in neuronal dendritic spines
[LiteratureReference:2682222] Crystal structure of human synbindin reveals two conformations of longin domain
modified[InstanceEdit:2867920] Jupe, S, 2012-12-19
[InstanceEdit:3597657] Jupe, S, 2013-05-22
textSyndecans have attached heparan sulfate (HS) and to a lesser extent chondroitin sulfate (CS) chains. These allow interactions with a large number of proteins. Various enzymes involved in post-translational HS chain modifications produce unique binding motifs that selectively recognize different proteins (Tkachenko et al. 2005). 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. Syndecans are also signalling molecules, interacting with cytoplasmic proteins. Syndecan-2 binds Trafficking protein particle complex subunit 4 (TRAPPC4), also known as synbindin. It appears to be involved with postsynaptic membrane trafficking (Ethell et al. 2000). Syndecan-2 expression promotes dendritic spine maturation in neurons, and requires the C2 domain (Ethell et al. 2000), suggesting that syndecan-2 and synbindin recruit intracellular vesicles to postsynaptic sites. More recently TRAPPC4 was shown to be a component of the Transport Protein Particle, involved in endoplasmic reticulum-to-Golgi transport (Fan et al. 2009).
(summation)[Reaction:2750175] Syndecan-2 binds Trappc4 [Mus musculus]
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