SDCBP

From Wikipedia, the free encyclopedia

Syndecan binding protein (syntenin)

PDB rendering based on 1n99.

Available structures: 1n99, 1nte, 1obx, 1oby, 1obz, 1r6j, 1v1t, 1w9e, 1w9o, 1w9q, 1ybo

Identifiers

Symbol(s)

SDCBP; MDA-9; ST1; SYCL; TACIP18

External IDs

OMIM: 602217 MGI: 1337026 HomoloGene: 4110

Gene ontology
Molecular Function:	• interleukin-5 receptor binding • protein binding • cytoskeletal adaptor activity • oxidoreductase activity • neurexin binding • syndecan binding • protein heterodimerization activity
Cellular Component:	• nucleus • endoplasmic reticulum • cytoskeleton • interleukin-5 receptor complex • adherens junction • membrane
Biological Process:	• protein targeting to membrane • substrate-bound cell migration, cell extension • intracellular signaling cascade • Ras protein signal transduction • synaptic transmission • metabolic process • actin cytoskeleton organization and biogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001007067 (mRNA)
NP_001007068 (protein)

NM_016807 (mRNA)
NP_058087 (protein)

Location

Chr 8: 59.63 - 59.66 Mb

Chr 4: 6.29 - 6.32 Mb

Pubmed search

[1]

[2]

Syndecan binding protein (syntenin), also known as SDCBP, is a human gene.

The protein encoded by this gene was initially identified as a molecule linking syndecan-mediated signaling to the cytoskeleton. The syntenin protein contains tandemly repeated PDZ domains that bind the cytoplasmic, C-terminal domains of a variety of transmembrane proteins. This protein may also affect cytoskeletal-membrane organization, cell adhesion, protein trafficking, and the activation of transcription factors. The protein is primarily localized to membrane-associated adherens junctions and focal adhesions but is also found at the endoplasmic reticulum and nucleus. Alternative splicing results in multiple transcript variants encoding different isoforms.^[1]

[edit] References

^ Entrez Gene: SDCBP syndecan binding protein (syntenin).

[edit] Further reading

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. PMID 12241528.
Harrod TR, Justement LB (2003). "Evaluating function of transmembrane protein tyrosine phosphatase CD148 in lymphocyte biology.". Immunol. Res. 26 (1-3): 153–66. PMID 12403354.
Sarkar D, Boukerche H, Su ZZ, Fisher PB (2005). "mda-9/syntenin: recent insights into a novel cell signaling and metastasis-associated gene.". Pharmacol. Ther. 104 (2): 101–15. doi:10.1016/j.pharmthera.2004.08.004. PMID 15518882.
"Letter: The condition of psychiatry." (1975). N. Engl. J. Med. 292 (18): 982. PMID 1117941.
Grootjans JJ, Zimmermann P, Reekmans G, et al. (1998). "Syntenin, a PDZ protein that binds syndecan cytoplasmic domains.". Proc. Natl. Acad. Sci. U.S.A. 94 (25): 13683–8. PMID 9391086.
Lin JJ, Jiang H, Fisher PB (1998). "Melanoma differentiation associated gene-9, mda-9, is a human gamma interferon responsive gene.". Gene 207 (2): 105–10. PMID 9511750.
Torres R, Firestein BL, Dong H, et al. (1999). "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands.". Neuron 21 (6): 1453–63. PMID 9883737.
Lin D, Gish GD, Songyang Z, Pawson T (1999). "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif.". J. Biol. Chem. 274 (6): 3726–33. PMID 9920925.
Fernández-Larrea J, Merlos-Suárez A, Ureña JM, et al. (1999). "A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface.". Mol. Cell 3 (4): 423–33. PMID 10230395.
Fialka I, Steinlein P, Ahorn H, et al. (1999). "Identification of syntenin as a protein of the apical early endocytic compartment in Madin-Darby canine kidney cells.". J. Biol. Chem. 274 (37): 26233–9. PMID 10473577.
Grootjans JJ, Reekmans G, Ceulemans H, David G (2000). "Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin.". J. Biol. Chem. 275 (26): 19933–41. doi:10.1074/jbc.M002459200. PMID 10770943.
Koroll M, Rathjen FG, Volkmer H (2001). "The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity.". J. Biol. Chem. 276 (14): 10646–54. doi:10.1074/jbc.M010647200. PMID 11152476.
Zimmermann P, Tomatis D, Rosas M, et al. (2001). "Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments.". Mol. Biol. Cell 12 (2): 339–50. PMID 11179419.
Jannatipour M, Dion P, Khan S, et al. (2001). "Schwannomin isoform-1 interacts with syntenin via PDZ domains.". J. Biol. Chem. 276 (35): 33093–100. doi:10.1074/jbc.M105792200. PMID 11432873.
Geijsen N, Uings IJ, Pals C, et al. (2001). "Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein.". Science 293 (5532): 1136–8. doi:10.1126/science.1059157. PMID 11498591.
Hirbec H, Perestenko O, Nishimune A, et al. (2002). "The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs.". J. Biol. Chem. 277 (18): 15221–4. doi:10.1074/jbc.C200112200. PMID 11891216.
Koo TH, Lee JJ, Kim EM, et al. (2002). "Syntenin is overexpressed and promotes cell migration in metastatic human breast and gastric cancer cell lines.". Oncogene 21 (26): 4080–8. doi:10.1038/sj.onc.1205514. PMID 12037664.
Biederer T, Sara Y, Mozhayeva M, et al. (2002). "SynCAM, a synaptic adhesion molecule that drives synapse assembly.". Science 297 (5586): 1525–31. doi:10.1126/science.1072356. PMID 12202822.