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Gene Review

SDCBP  -  syndecan binding protein (syntenin)

Homo sapiens

Synonyms: MDA-9, MDA9, Melanoma differentiation-associated protein 9, Pro-TGF-alpha cytoplasmic domain-interacting protein 18, ST1, ...
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Disease relevance of SDCBP

  • Syntenin, a 33 kDa protein, interacts with several cell membrane receptors and with merlin, the product of the causal gene for neurofibromatosis type II [1].
  • A recently identified member of this protein family is melanoma differentiation associated gene-9 (mda-9), also known as syntenin, which was first identified as a gene down-regulated during human melanoma differentiation as mda-9 and subsequently recognized as an interacting partner of the cell-surface heparan sulfate syndecans, syntenin [2].
  • Interest in mda-9/syntenin is intensifying because of its involvement in organization of protein complexes in the plasma membranes, regulation of B cell development, intracellular trafficking and cell surface targeting, cancer metastasis, synaptic transmission, and axonal outgrowth [2].
  • In this review, we discuss the identification, structure and function of mda-9/syntenin and delineate future studies to address its role in regulating key physiological and pathological processes [2].
  • Regulating mda-9/syntenin expression using a replication-incompetent adenovirus expressing either sense or antisense mda-9/syntenin modifies the transformed phenotype and alters metastatic ability in immortal human melanocytes and metastatic melanoma cells in vitro and in vivo in newborn rats [3].

High impact information on SDCBP


Chemical compound and disease context of SDCBP


Biological context of SDCBP


Anatomical context of SDCBP

  • Recombinant domains of syntenin with the highest plasma membrane localization display the lowest nuclear localization [10].
  • Syntenin is an adapter protein that couples transmembrane proteoglycans to cytoskeletal components and is involved in intracellular vesicle transport [11].
  • The addition of a segment of 10 amino acids from the N-terminal domain of syntenin to these PDZ domains increases the localization of the tags to stress fibers and induces the formation of long, branching plasma membrane extensions [10].
  • Fibroblast cells expressing heterologous antisense syntenin display alterations in the subcellular distribution of sch-1 [11].
  • Lastly, syntenin and ephrin B1 could be co-immunoprecipitated from transfected COS-1 cells, suggesting that PDZ domain binding of B ephrins can occur in cells [12].

Associations of SDCBP with chemical compounds


Physical interactions of SDCBP

  • Here we provide evidence that each PDZ domain of syntenin can interact with a syndecan [9].
  • The paired, but not the isolated PDZ domains of syntenin bind also strongly to the immobilized cytoplasmic domains of neurexin and B-class ephrins [9].
  • In addition, the C terminus of syntenin-1 has a stabilizing role in the CD63-syntenin-1 association, as deletion of the last 17 amino acids abolished the interaction [16].

Other interactions of SDCBP

  • Our results demonstrated that eIF5A and syntenin could engage in a specific interaction both in vitro and in vivo and functioned collaboratively to regulate p53 activity [17].
  • In vitro studies demonstrated that the fifth PDZ domain of FAP-1 and full-length syntenin bound ephrin B1 via the carboxyl-terminal motif [12].
  • mda-9/syntenin: recent insights into a novel cell signaling and metastasis-associated gene [2].
  • These findings suggest that ST1 expression in breast cancer tissue is irrespective of the expression of the extracellular matrix component, the proteolytic enzyme cathepsin D and the growth fraction of the tumour, and that it could be a potential new prognostic marker in breast cancer [18].
  • Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5 receptor (alpha chain) and syndecan, reveal the molecular roots of syntenin's degenerate specificity [19].

Analytical, diagnostic and therapeutic context of SDCBP


  1. PDZ tandem of human syntenin: crystal structure and functional properties. Kang, B.S., Cooper, D.R., Jelen, F., Devedjiev, Y., Derewenda, U., Dauter, Z., Otlewski, J., Derewenda, Z.S. Structure (Camb.) (2003) [Pubmed]
  2. mda-9/syntenin: recent insights into a novel cell signaling and metastasis-associated gene. Sarkar, D., Boukerche, H., Su, Z.Z., Fisher, P.B. Pharmacol. Ther. (2004) [Pubmed]
  3. mda-9/Syntenin: a positive regulator of melanoma metastasis. Boukerche, H., Su, Z.Z., Emdad, L., Baril, P., Balme, B., Thomas, L., Randolph, A., Valerie, K., Sarkar, D., Fisher, P.B. Cancer Res. (2005) [Pubmed]
  4. Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein. Geijsen, N., Uings, I.J., Pals, C., Armstrong, J., McKinnon, M., Raaijmakers, J.A., Lammers, J.W., Koenderman, L., Coffer, P.J. Science (2001) [Pubmed]
  5. PIP(2)-PDZ domain binding controls the association of syntenin with the plasma membrane. Zimmermann, P., Meerschaert, K., Reekmans, G., Leenaerts, I., Small, J.V., Vandekerckhove, J., David, G., Gettemans, J. Mol. Cell (2002) [Pubmed]
  6. Nuclear speckles and nucleoli targeting by PIP2-PDZ domain interactions. Mortier, E., Wuytens, G., Leenaerts, I., Hannes, F., Heung, M.Y., Degeest, G., David, G., Zimmermann, P. EMBO J. (2005) [Pubmed]
  7. Syntenin, a PDZ protein that binds syndecan cytoplasmic domains. Grootjans, J.J., Zimmermann, P., Reekmans, G., Smets, A., Degeest, G., Dürr, J., David, G. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  8. Evaluation of non-radioactive trivalent DNA probe (LT, ST1a, ST1b) for detecting enterotoxigenic Escherichia coli. Chapman, P.A., Daly, C.M. J. Clin. Pathol. (1993) [Pubmed]
  9. Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin. Grootjans, J.J., Reekmans, G., Ceulemans, H., David, G. J. Biol. Chem. (2000) [Pubmed]
  10. Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments. Zimmermann, P., Tomatis, D., Rosas, M., Grootjans, J., Leenaerts, I., Degeest, G., Reekmans, G., Coomans, C., David, G. Mol. Biol. Cell (2001) [Pubmed]
  11. Schwannomin isoform-1 interacts with syntenin via PDZ domains. Jannatipour, M., Dion, P., Khan, S., Jindal, H., Fan, X., Laganière, J., Chishti, A.H., Rouleau, G.A. J. Biol. Chem. (2001) [Pubmed]
  12. The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif. Lin, D., Gish, G.D., Songyang, Z., Pawson, T. J. Biol. Chem. (1999) [Pubmed]
  13. The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs. Hirbec, H., Perestenko, O., Nishimune, A., Meyer, G., Nakanishi, S., Henley, J.M., Dev, K.K. J. Biol. Chem. (2002) [Pubmed]
  14. Syndecan recycling [corrected] is controlled by syntenin-PIP2 interaction and Arf6. Zimmermann, P., Zhang, Z., Degeest, G., Mortier, E., Leenaerts, I., Coomans, C., Schulz, J., N'Kuli, F., Courtoy, P.J., David, G. Dev. Cell (2005) [Pubmed]
  15. The tyrosine kinase inhibitor CGP 57148 (ST1 571) induces apoptosis in BCR-ABL-positive cells by down-regulating BCL-X. Oetzel, C., Jonuleit, T., Götz, A., van der Kuip, H., Michels, H., Duyster, J., Hallek, M., Aulitzky, W.E. Clin. Cancer Res. (2000) [Pubmed]
  16. Syntenin-1 Is a New Component of Tetraspanin-Enriched Microdomains: Mechanisms and Consequences of the Interaction of Syntenin-1 with CD63. Latysheva, N., Muratov, G., Rajesh, S., Padgett, M., Hotchin, N.A., Overduin, M., Berditchevski, F. Mol. Cell. Biol. (2006) [Pubmed]
  17. A novel eIF5A complex functions as a regulator of p53 and p53-dependent apoptosis. Li, A.L., Li, H.Y., Jin, B.F., Ye, Q.N., Zhou, T., Yu, X.D., Pan, X., Man, J.H., He, K., Yu, M., Hu, M.R., Wang, J., Yang, S.C., Shen, B.F., Zhang, X.M. J. Biol. Chem. (2004) [Pubmed]
  18. Matrix metalloproteinase expression in human breast cancer: an immunohistochemical study including correlation with cathepsin D, type IV collagen, laminin, fibronectin, EGFR, c-erbB-2 oncoprotein, p53, steroid receptors status and proliferative indices. Ioachim, E.E., Athanassiadou, S.E., Kamina, S., Carassavoglou, K., Agnantis, N.J. Anticancer Res. (1998) [Pubmed]
  19. Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm. Kang, B.S., Cooper, D.R., Devedjiev, Y., Derewenda, U., Derewenda, Z.S. Structure (Camb.) (2003) [Pubmed]
  20. The PDZ2 domain of syntenin at ultra-high resolution: bridging the gap between macromolecular and small molecule crystallography. Kang, B.S., Devedjiev, Y., Derewenda, U., Derewenda, Z.S. J. Mol. Biol. (2004) [Pubmed]
  21. Melanoma metastasis is associated with enhanced expression of the syntenin gene. Helmke, B.M., Polychronidis, M., Benner, A., Thome, M., Arribas, J., Deichmann, M. Oncol. Rep. (2004) [Pubmed]
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