SDC4

Syndecan 4

PDB rendering based on 1ejp.

Available structures
PDB	1EJP, 1EJQ, 1OBY, 1YBO

Identifiers

Symbols

SDC4; MGC22217; SYND4

External IDs

OMIM: 600017 MGI: 1349164 HomoloGene: 31121 GeneCards: SDC4 Gene

Gene Ontology
Molecular function	• fibronectin binding • protein kinase C binding • cytoskeletal protein binding • thrombospondin receptor activity
Cellular component	• extracellular region • integral to plasma membrane • focal adhesion • cell surface • membrane • costamere • membrane raft
Biological process	• ureteric bud development • biological_process • positive regulation of protein kinase activity • positive regulation of stress fiber assembly • positive regulation of focal adhesion assembly
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 20:
43.95 – 43.98 Mb

Chr 2:
164.25 – 164.27 Mb

PubMed search

[1]

[2]

Syndecan-4 is a protein that in humans is encoded by the SDC4 gene.^[1]^[2]

1 Gene
2 Function
3 Clinical significance
- 3.1 Osteoarthritis
4 References
5 Further reading

Gene

This gene is found on chromosome 20, while a pseudogene has been found on chromosome 22.^[3]

Function

Syndecan-4 is a transmembrane (type I) heparan sulfate proteoglycan that functions as a receptor in intracellular signaling. The protein is found as a homodimer and is a member of the syndecan proteoglycan family.^[3]

Clinical significance

Osteoarthritis

Syndecan-4 is upregulated in osteoarthritis and inhibition of syndecan-4 reduces cartilage destruction in mouse models of OA.^[4]

See Sindecán-4 at the spanish Wikipedia

References

^ Kojima T, Inazawa J, Takamatsu J, Rosenberg RD, Saito H (Mar 1993). "Human ryudocan core protein: molecular cloning and characterization of the cDNA, and chromosomal localization of the gene". Biochem Biophys Res Commun 190 (3): 814–22. doi:10.1006/bbrc.1993.1122. PMID 7916598.
^ David G, van der Schueren B, Marynen P, Cassiman JJ, van den Berghe H (Sep 1992). "Molecular cloning of amphiglycan, a novel integral membrane heparan sulfate proteoglycan expressed by epithelial and fibroblastic cells". J Cell Biol 118 (4): 961–9. doi:10.1083/jcb.118.4.961. PMC 2289559. PMID 1500433. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289559.
^ ^a ^b "Entrez Gene: SDC4 syndecan 4". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6385.
^ Hass MJ (Sept 2009). "SDC4: OA joint effort". SciBX 2 (34). doi:10.1038/scibx.2009.1297.

Bass MD, Humphries MJ (2002). "Cytoplasmic interactions of syndecan-4 orchestrate adhesion receptor and growth factor receptor signalling". Biochem. J. 368 (Pt 1): 1–15. doi:10.1042/BJ20021228. PMC 1222989. PMID 12241528. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222989.
Yu H, Humphries DE, Watkins M, Karlinsky JB (1995). "Molecular cloning of the human ryudocan promoter". Biochem. Biophys. Res. Commun. 212 (3): 1139–44. doi:10.1006/bbrc.1995.2087. PMID 7626103.
Barillari G, Gendelman R, Gallo RC, Ensoli B (1993). "The Tat protein of human immunodeficiency virus type 1, a growth factor for AIDS Kaposi sarcoma and cytokine-activated vascular cells, induces adhesion of the same cell types by using integrin receptors recognizing the RGD amino acid sequence". Proc. Natl. Acad. Sci. U.S.A. 90 (17): 7941–5. doi:10.1073/pnas.90.17.7941. PMC 47263. PMID 7690138. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=47263.
Woods A, Couchman JR (1994). "Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component". Mol. Biol. Cell 5 (2): 183–92. PMC 301024. PMID 8019004. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=301024.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Albini A, Benelli R, Presta M, et al. (1996). "HIV-tat protein is a heparin-binding angiogenic growth factor". Oncogene 12 (2): 289–97. PMID 8570206.
Kojima T, Katsumi A, Yamazaki T, et al. (1996). "Human ryudocan from endothelium-like cells binds basic fibroblast growth factor, midkine, and tissue factor pathway inhibitor". J. Biol. Chem. 271 (10): 5914–20. doi:10.1074/jbc.271.10.5914. PMID 8621465.
Takagi A, Kojima T, Tsuzuki S, et al. (1997). "Structural organization and promoter activity of the human ryudocan gene". J. Biochem. 119 (5): 979–84. PMID 8797100.
Rusnati M, Coltrini D, Oreste P, et al. (1997). "Interaction of HIV-1 Tat protein with heparin. Role of the backbone structure, sulfation, and size". J. Biol. Chem. 272 (17): 11313–20. doi:10.1074/jbc.272.17.11313. PMID 9111037.
Chang HC, Samaniego F, Nair BC, et al. (1997). "HIV-1 Tat protein exits from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region". AIDS 11 (12): 1421–31. doi:10.1097/00002030-199712000-00006. PMID 9342064.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Horowitz A, Simons M (1998). "Regulation of syndecan-4 phosphorylation in vivo". J. Biol. Chem. 273 (18): 10914–8. doi:10.1074/jbc.273.18.10914. PMID 9556568.
Lee D, Oh ES, Woods A, et al. (1998). "Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate". J. Biol. Chem. 273 (21): 13022–9. doi:10.1074/jbc.273.21.13022. PMID 9582338.
Cohen AR, Woods DF, Marfatia SM, et al. (1998). "Human CASK/LIN-2 Binds Syndecan-2 and Protein 4.1 and Localizes to the Basolateral Membrane of Epithelial Cells". J. Cell Biol. 142 (1): 129–38. doi:10.1083/jcb.142.1.129. PMC 2133028. PMID 9660868. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133028.
Rusnati M, Tulipano G, Spillmann D, et al. (1999). "Multiple interactions of HIV-I Tat protein with size-defined heparin oligosaccharides". J. Biol. Chem. 274 (40): 28198–205. doi:10.1074/jbc.274.40.28198. PMID 10497173.
Gao Y, Li M, Chen W, Simons M (2000). "Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration". J. Cell. Physiol. 184 (3): 373–9. doi:10.1002/1097-4652(200009)184:3<373::AID-JCP12>3.0.CO;2-I. PMID 10911369.
Tyagi M, Rusnati M, Presta M, Giacca M (2001). "Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans". J. Biol. Chem. 276 (5): 3254–61. doi:10.1074/jbc.M006701200. PMID 11024024.
Shin J, Lee W, Lee D, et al. (2001). "Solution structure of the dimeric cytoplasmic domain of syndecan-4". Biochemistry 40 (29): 8471–8. doi:10.1021/bi002750r. PMID 11456484.

PDB gallery

1ejp: SOLUTION STRUCTURE OF THE SYNDECAN-4 WHOLE CYTOPLASMIC DOMAIN

1ejq: SOLUTION STRUCTURE OF THE SYNDECAN-4 WHOLE CYTOPLASMIC DOMAIN IN THE PRESENCE OF PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE