Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person Syndecans are type I transmembrane proteins, with an N-termi...
| Class:Id | Summation:2867910 |
|---|---|
| _displayName | Syndecans are type I transmembrane proteins, with an N-termi... |
| _timestamp | 2012-12-19 13:36:18 |
| created | [InstanceEdit:2867911] Jupe, S, 2012-12-19 |
| 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:2684472] Heparan sulfate proteoglycans from mouse mammary epithelial cells. Cell surface proteoglycan as a receptor for interstitial collagens |
| 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. 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 several types of collagen (type I, III and V Koda et al. 1985). |
| [Change default viewing format] | |
No pathways have been reviewed or authored by Syndecans are type I transmembrane proteins, with an N-termi... (2867910)
