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Volumn 121, Issue 9, 2008, Pages 1349-1355

The ins and outs of syntenin, a multifunctional intracellular adaptor protein

Author keywords

Adaptor; PDZ domain; Syntenin

Indexed keywords

BETA NEUREXIN; CD6 ANTIGEN; CD63 ANTIGEN; EPHRIN; EPHRIN RECEPTOR; FASCIN; FOCAL ADHESION KINASE; FRIZZLED PROTEIN; GLUTAMATE RECEPTOR; GLYCINE TRANSPORTER 2; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INITIATION FACTOR 5A; INTERLEUKIN 5 RECEPTOR ALPHA; MERLIN; MITOGEN ACTIVATED PROTEIN KINASE P38; NEUREXIN; POSTSYNAPTIC DENSITY PROTEIN 95; PROTEIN INTERACTING WITH PROTEIN KINASE C; PROTEIN TYROSINE PHOSPHATASE; RAB7 PROTEIN; STRESS ACTIVATED PROTEIN KINASE; SYNDECAN; SYNTAXIN 1; SYNTENIN; TRANSFORMING GROWTH FACTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UNCOUPLING PROTEIN; UNCOUPLING PROTEIN 51; WNT PROTEIN;

EID: 46649120323     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.026401     Document Type: Article
Times cited : (103)

References (47)
  • 3
    • 33847748493 scopus 로고    scopus 로고
    • mda-9/Syntenin regulates the metastatic phenotype in human melanoma cells by activating nuclear factor-kappaB
    • Boukerche, H., Su, Z. Z., Emdad, L., Sarkar, D. and Fisher, P. B. (2007). mda-9/Syntenin regulates the metastatic phenotype in human melanoma cells by activating nuclear factor-kappaB. Cancer Res. 67, 1812-1822.
    • (2007) Cancer Res , vol.67 , pp. 1812-1822
    • Boukerche, H.1    Su, Z.Z.2    Emdad, L.3    Sarkar, D.4    Fisher, P.B.5
  • 5
  • 6
    • 13844281177 scopus 로고    scopus 로고
    • Probing the supramodular architecture of a multidomain protein: The structure of syntenin in solution
    • Cierpicki, T., Bushweller, J. H. and Derewenda, Z. S. (2005). Probing the supramodular architecture of a multidomain protein: the structure of syntenin in solution. Structure 13, 319-327.
    • (2005) Structure , vol.13 , pp. 319-327
    • Cierpicki, T.1    Bushweller, J.H.2    Derewenda, Z.S.3
  • 7
    • 33846615765 scopus 로고    scopus 로고
    • The trick ofthe tail: Protein-protein interactions of metabotropic glutamate receptors
    • Enz, R. (2007). The trick ofthe tail: protein-protein interactions of metabotropic glutamate receptors. BioEssays 29, 60-73.
    • (2007) BioEssays , vol.29 , pp. 60-73
    • Enz, R.1
  • 8
    • 0037616361 scopus 로고    scopus 로고
    • Different binding motifs in metabotropic glutamate receptor type 7b for filamin A, protein phosphatase 1C, protein interacting with protein kinase C (PICK) 1 and syntenin allow the formation ofmultimeric protein complexes
    • Enz, R. and Croci, C. (2003). Different binding motifs in metabotropic glutamate receptor type 7b for filamin A, protein phosphatase 1C, protein interacting with protein kinase C (PICK) 1 and syntenin allow the formation ofmultimeric protein complexes. Biochem. J. 372, 183-191.
    • (2003) Biochem. J , vol.372 , pp. 183-191
    • Enz, R.1    Croci, C.2
  • 9
    • 34548574739 scopus 로고    scopus 로고
    • Syntenin mediates Delta1-induced cohesiveness of epidermal stem cells in culture
    • Estrach, S., Legg, J. and Watt, F. M. (2007). Syntenin mediates Delta1-induced cohesiveness of epidermal stem cells in culture. J. Cell Sci. 120, 2944-2952.
    • (2007) J. Cell Sci , vol.120 , pp. 2944-2952
    • Estrach, S.1    Legg, J.2    Watt, F.M.3
  • 10
    • 0033120592 scopus 로고    scopus 로고
    • A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface
    • Fernandez-Larrea, J., Merlos-Suarez, A., Urena, J. M., Baselga, J. and Arribas, J. (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, 423-433.
    • (1999) Mol. Cell , vol.3 , pp. 423-433
    • Fernandez-Larrea, J.1    Merlos-Suarez, A.2    Urena, J.M.3    Baselga, J.4    Arribas, J.5
  • 15
    • 0034733733 scopus 로고    scopus 로고
    • Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin
    • Grootjans, J. J., Reekmans, G., Ceulemans, H. and David, G. (2000). Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin. J. Biol. Chem. 275, 19933-19941.
    • (2000) J. Biol. Chem , vol.275 , pp. 19933-19941
    • Grootjans, J.J.1    Reekmans, G.2    Ceulemans, H.3    David, G.4
  • 16
    • 0036397494 scopus 로고    scopus 로고
    • Evaluating function of transmembrane protein tyrosine phosphatase CD148 in lymphocyte biology
    • Harrod, T. R. and Justement, L. B. (2002). Evaluating function of transmembrane protein tyrosine phosphatase CD148 in lymphocyte biology. Immunol. Res. 26, 153-166.
    • (2002) Immunol. Res , vol.26 , pp. 153-166
    • Harrod, T.R.1    Justement, L.B.2
  • 17
    • 16544367970 scopus 로고    scopus 로고
    • Melanoma metastasis is associated with enhanced expression of the syntenin gene
    • Helmke, B. M., Polychronidis, M., Benner, A., Thome, M., Arribas, J. and Deichmann, M. (2004). Melanoma metastasis is associated with enhanced expression of the syntenin gene. Oncol. Rep. 12, 221-228.
    • (2004) Oncol. Rep , vol.12 , pp. 221-228
    • Helmke, B.M.1    Polychronidis, M.2    Benner, A.3    Thome, M.4    Arribas, J.5    Deichmann, M.6
  • 18
    • 0037013318 scopus 로고    scopus 로고
    • The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis ofPDZ binding motifs
    • Hirbec, H., Perestenko, O., Nishimune, A., Meyer, G., Nakanishi, S., Henley, J. M. and Dev, K. K. (2002). The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis ofPDZ binding motifs. J. Biol. Chem. 277, 15221-15224.
    • (2002) J. Biol. Chem , vol.277 , pp. 15221-15224
    • Hirbec, H.1    Perestenko, O.2    Nishimune, A.3    Meyer, G.4    Nakanishi, S.5    Henley, J.M.6    Dev, K.K.7
  • 20
    • 15244360313 scopus 로고    scopus 로고
    • Syntenin is involved in the developmental regulation of neuronal membrane architecture
    • Hirbec, H., Martin, S. and Henley, J. M. (2005). Syntenin is involved in the developmental regulation of neuronal membrane architecture. Mol. Cell. Neurosci. 28, 737-746.
    • (2005) Mol. Cell. Neurosci , vol.28 , pp. 737-746
    • Hirbec, H.1    Martin, S.2    Henley, J.M.3
  • 23
    • 24344449035 scopus 로고    scopus 로고
    • Role of the endocytic machinery in the sorting of lysosome-associated membrane proteins
    • Janvier, K. and Bonifacino, J. S. (2005). Role of the endocytic machinery in the sorting of lysosome-associated membrane proteins. Mol. Biol. Cell 16, 4231-4242.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4231-4242
    • Janvier, K.1    Bonifacino, J.S.2
  • 24
    • 0037816293 scopus 로고    scopus 로고
    • 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. and Derewenda, Z. S. (2003a). Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm. Structure 11, 845-853.
    • (2003) Structure , vol.11 , pp. 845-853
    • Kang, B.S.1    Cooper, D.R.2    Devedjiev, Y.3    Derewenda, U.4    Derewenda, Z.S.5
  • 26
    • 32544447532 scopus 로고    scopus 로고
    • Organization of the presynaptic active zone by ERC2/CAST1-dependent clustering of the tandem PDZ protein syntenin-1
    • Ko, J., Yoon, C., Piccoli, G., Chung, H. S., Kim, K., Lee, J. R., Lee, H. W., Kim, H., Sala, C. and Kim, E. (2006). Organization of the presynaptic active zone by ERC2/CAST1-dependent clustering of the tandem PDZ protein syntenin-1. J. Neurosci. 26, 963-970.
    • (2006) J. Neurosci , vol.26 , pp. 963-970
    • Ko, J.1    Yoon, C.2    Piccoli, G.3    Chung, H.S.4    Kim, K.5    Lee, J.R.6    Lee, H.W.7    Kim, H.8    Sala, C.9    Kim, E.10
  • 28
    • 0037071898 scopus 로고    scopus 로고
    • Syntenin is overexpressed and promotes cell migration in metastatic human breast and gastric cancer cell lines
    • Koo, T. H., Lee, J. J., Kim, E. M., Vim, K. W., Kim, H. D. and Lee, J. H. (2002). Syntenin is overexpressed and promotes cell migration in metastatic human breast and gastric cancer cell lines. Oncogene 21, 4080-4088.
    • (2002) Oncogene , vol.21 , pp. 4080-4088
    • Koo, T.H.1    Lee, J.J.2    Kim, E.M.3    Vim, K.W.4    Kim, H.D.5    Lee, J.H.6
  • 29
    • 0035815656 scopus 로고    scopus 로고
    • The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity
    • Koroll, M., Rathjen, F. G. and 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, 10646-10654.
    • (2001) J. Biol. Chem , vol.276 , pp. 10646-10654
    • Koroll, M.1    Rathjen, F.G.2    Volkmer, H.3
  • 30
    • 33749635768 scopus 로고    scopus 로고
    • Syritenin-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. and Berditchevski, F. (2006). Syritenin-1 is a new component of tetraspanin-enriched microdomains: mechanisms and consequences of the interaction of syntenin-1 with CD63. Mol. Cell. Biol. 26, 7707-7718.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 7707-7718
    • Latysheva, N.1    Muratov, G.2    Rajesh, S.3    Padgett, M.4    Hotchin, N.A.5    Overduin, M.6    Berditchevski, F.7
  • 31
    • 10344232013 scopus 로고    scopus 로고
    • A novel cIF5A 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. et al. (2004). A novel cIF5A complex functions as a regulator of p53 and p53-dependent apoptosis. J. Biol. Chem. 279, 49251-49258.
    • (2004) J. Biol. Chem , vol.279 , pp. 49251-49258
    • Li, A.L.1    Li, H.Y.2    Jin, B.F.3    Ye, Q.N.4    Zhou, T.5    Yu, X.D.6    Pan, X.7    Man, J.H.8    He, K.9    Yu, M.10
  • 32
    • 0033525063 scopus 로고    scopus 로고
    • The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif
    • Lin, D., Gish, G. D., Songyang, Z. and Pawson, T. (1999). The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif. J. Biol. Chem. 274, 3726-3733.
    • (1999) J. Biol. Chem , vol.274 , pp. 3726-3733
    • Lin, D.1    Gish, G.D.2    Songyang, Z.3    Pawson, T.4
  • 33
    • 0032579216 scopus 로고    scopus 로고
    • Melanoma differentiation associated gene-9, mda-9, is a human gamma interferon responsive gene
    • Lin, J. J., Jiang, H. and Fisher, P. B. (1998). Melanoma differentiation associated gene-9, mda-9, is a human gamma interferon responsive gene. Gene 207, 105-110.
    • (1998) Gene , vol.207 , pp. 105-110
    • Lin, J.J.1    Jiang, H.2    Fisher, P.B.3
  • 37
    • 3242756821 scopus 로고    scopus 로고
    • The neuronal glycine transporter 2 interacts with the PDZ domain protein syntenin-1
    • Ohno, K., Koroll, M., El Far, O., Schulze, P., Gomeza, J. and Betz, H. (2004). The neuronal glycine transporter 2 interacts with the PDZ domain protein syntenin-1. Mol. Cell. Neurosci. 26, 518-529.
    • (2004) Mol. Cell. Neurosci , vol.26 , pp. 518-529
    • Ohno, K.1    Koroll, M.2    El Far, O.3    Schulze, P.4    Gomeza, J.5    Betz, H.6
  • 38
    • 0035139220 scopus 로고    scopus 로고
    • The neuronal Rho-GEF Kalirin-7 interacts with PDZ domain-containing proteins and regulates dendritic morphogenesis
    • Penzes, P., Johnson, R. C., Sattler, R., Zhang, X., Huganir, R. L., Kambampati V., Mains, R. E. and Eipper, B. A. (2001). The neuronal Rho-GEF Kalirin-7 interacts with PDZ domain-containing proteins and regulates dendritic morphogenesis. Neuron 29, 229-242.
    • (2001) Neuron , vol.29 , pp. 229-242
    • Penzes, P.1    Johnson, R.C.2    Sattler, R.3    Zhang, X.4    Huganir, R.L.5    Kambampati, V.6    Mains, R.E.7    Eipper, B.A.8
  • 39
    • 7244245840 scopus 로고    scopus 로고
    • mda-9/syntenin: Recent insights into a novel cell signaling and metastasis-associated gene
    • Sarkar, D., Boukerche, H., Su, Z. Z. and Fisher, P. B. (2004). mda-9/syntenin: recent insights into a novel cell signaling and metastasis-associated gene. Pharmacol. Ther. 104, 101-115.
    • (2004) Pharmacol. Ther , vol.104 , pp. 101-115
    • Sarkar, D.1    Boukerche, H.2    Su, Z.Z.3    Fisher, P.B.4
  • 40
    • 37449027708 scopus 로고    scopus 로고
    • Structural insights into the PIP2 recognition by symenin-1 PDZ domain
    • Sugi, T., Oyama, T., Morikawa, K. and Jingami, H. (2008). Structural insights into the PIP2 recognition by symenin-1 PDZ domain. Biochem. Biophys. Res. Commun. 366, 373-378.
    • (2008) Biochem. Biophys. Res. Commun , vol.366 , pp. 373-378
    • Sugi, T.1    Oyama, T.2    Morikawa, K.3    Jingami, H.4
  • 41
    • 1642417689 scopus 로고    scopus 로고
    • Role of Unc51.1 and its binding partners in CNS axon outgrowth
    • Tomoda, T., Kim, J. H., Zhan, C. and Hatten, M. E. (2004). Role of Unc51.1 and its binding partners in CNS axon outgrowth. Genes Dev. 18, 541-558.
    • (2004) Genes Dev , vol.18 , pp. 541-558
    • Tomoda, T.1    Kim, J.H.2    Zhan, C.3    Hatten, M.E.4
  • 43
    • 0037070149 scopus 로고    scopus 로고
    • PDZ domains: Troubles in classification
    • Vaccaro, P. and Dente, L. (2002). PDZ domains: troubles in classification. FEBS Lett. 512, 345-349.
    • (2002) FEBS Lett , vol.512 , pp. 345-349
    • Vaccaro, P.1    Dente, L.2
  • 44
    • 33748313081 scopus 로고    scopus 로고
    • The prevalence and significance of PDZ domain-phosphoinositide interactions
    • Zimmermann, P. (2006). The prevalence and significance of PDZ domain-phosphoinositide interactions. Biochim. Biophys. Acta 1761, 947-956.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 947-956
    • Zimmermann, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.