SDCBP
| Syndecan binding protein (syntenin) |
PDB rendering based on 1n99. |
| Available structures |
| PDB |
1N99, 1NTE, 1OBX, 1OBY, 1OBZ, 1R6J, 1V1T, 1W9E, 1W9O, 1W9Q, 1YBO |
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| Identifiers |
| Symbols |
SDCBP; MDA-9; ST1; SYCL; TACIP18 |
| External IDs |
OMIM: 602217 MGI: 1337026 HomoloGene: 4110 GeneCards: SDCBP Gene |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
6386 |
53378 |
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| Ensembl |
ENSG00000137575 |
ENSMUSG00000028249 |
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| UniProt |
O00560 |
Q3TET7 |
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| RefSeq (mRNA) |
NM_001007067.1 |
NM_016807 |
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| RefSeq (protein) |
NP_001007068.1 |
NP_058087 |
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| Location (UCSC) |
Chr 8:
59.47 – 59.5 Mb |
Chr 4:
6.29 – 6.34 Mb |
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| PubMed search |
[1] |
[2] |
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Syntenin-1 is a protein that in humans is encoded by the SDCBP gene.[1]
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.[2]
Interactions
SDCBP has been shown to interact with Merlin,[3] ULK1,[4] Interleukin 5 receptor alpha subunit,[5] SOX4,[5] RAB5A,[4] EFNB1,[6] TRAF6,[7] GRIK1[8] and GRIK2.[8][9]
References
- ^ Grootjans JJ, Zimmermann P, Reekmans G, Smets A, Degeest G, Durr J, David G (January 1998). "Syntenin, a PDZ protein that binds syndecan cytoplasmic domains". Proc Natl Acad Sci USA 94 (25): 13683–8. doi:10.1073/pnas.94.25.13683. PMC 28366. PMID 9391086. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=28366.
- ^ "Entrez Gene: SDCBP syndecan binding protein (syntenin)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6386.
- ^ Jannatipour, M; Dion P, Khan S, Jindal H, Fan X, Laganière J, Chishti A H, Rouleau G A (August 2001). "Schwannomin isoform-1 interacts with syntenin via PDZ domains". J. Biol. Chem. (United States) 276 (35): 33093–100. doi:10.1074/jbc.M105792200. ISSN 0021-9258. PMID 11432873.
- ^ a b Tomoda, Toshifumi; Kim Jee Hae, Zhan Caixin, Hatten Mary E (March 2004). "Role of Unc51.1 and its binding partners in CNS axon outgrowth". Genes Dev. (United States) 18 (5): 541–58. doi:10.1101/gad.1151204. ISSN 0890-9369. PMC 374236. PMID 15014045. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=374236.
- ^ a b Geijsen, N; Uings I J, Pals C, Armstrong J, McKinnon M, Raaijmakers J A, Lammers J W, Koenderman L, Coffer P J (August 2001). "Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein". Science (United States) 293 (5532): 1136–8. doi:10.1126/science.1059157. ISSN 0036-8075. PMID 11498591.
- ^ Lin, D; Gish G D, Songyang Z, Pawson T (February 1999). "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif". J. Biol. Chem. (UNITED STATES) 274 (6): 3726–33. doi:10.1074/jbc.274.6.3726. ISSN 0021-9258. PMID 9920925.
- ^ Chen, Fang; Du Yijuan, Zhang Zheng, Chen Gang, Zhang Min, Shu Hong-Bing, Zhai Zhonghe, Chen Danying (April 2008). "Syntenin negatively regulates TRAF6-mediated IL-1R/TLR4 signaling". Cell. Signal. (England) 20 (4): 666–74. doi:10.1016/j.cellsig.2007.12.002. ISSN 0898-6568. PMID 18234474.
- ^ a b Hirbec, Hélène; Francis Joanna C, Lauri Sari E, Braithwaite Steven P, Coussen Françoise, Mulle Christophe, Dev Kumlesh K, Coutinho Victoria, Meyer Guido, Isaac John T R, Collingridge Graham L, Henley Jeremy M, Couthino Victoria (February 2003). "Rapid and differential regulation of AMPA and kainate receptors at hippocampal mossy fibre synapses by PICK1 and GRIP". Neuron (United States) 37 (4): 625–38. doi:10.1016/S0896-6273(02)01191-1. ISSN 0896-6273. PMID 12597860.
- ^ Hirbec, Hélène; Perestenko Olga, Nishimune Atsushi, Meyer Guido, Nakanishi Shigetada, Henley Jeremy M, Dev Kumlesh K (May 2002). "The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs". J. Biol. Chem. (United States) 277 (18): 15221–4. doi:10.1074/jbc.C200112200. ISSN 0021-9258. PMID 11891216.
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. PMC 1222989. PMID 12241528. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222989.
- Harrod TR, Justement LB (2003). "Evaluating function of transmembrane protein tyrosine phosphatase CD148 in lymphocyte biology.". Immunol. Res. 26 (1-3): 153–66. doi:10.1385/IR:26:1-3:153. 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.". N. Engl. J. Med. 292 (18): 982. 1975. doi:10.1056/NEJM197505012921826. PMID 1117941.
- 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. doi:10.1016/S0378-1119(97)00562-3. 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. doi:10.1016/S0896-6273(00)80663-7. 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. doi:10.1074/jbc.274.6.3726. 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. doi:10.1016/S1097-2765(00)80470-0. 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. doi:10.1074/jbc.274.37.26233. 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. PMC 30947. PMID 11179419. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=30947.
- 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.
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PDB gallery
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1n99: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN
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1nte: CRYSTAL STRUCTURE ANALYSIS OF THE SECOND PDZ DOMAIN OF SYNTENIN
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1obx: CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.
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1oby: CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH A SYNDECAN-4 PEPTIDE.
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1obz: CRYSTAL STRUCTURE OF THE COMPLEX OF THE PDZ TANDEM OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.
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1r6j: Ultrahigh resolution Crystal Structure of syntenin PDZ2
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1v1t: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEYKV PEPTIDE
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1w9e: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEFYF PEPTIDE
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1w9o: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEYYV PEPTIDE
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1w9q: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEFAF PEPTIDE
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1ybo: Crystal structure of the PDZ tandem of human syntenin with syndecan peptide
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