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Gene Review

TUSC2  -  tumor suppressor candidate 2

Homo sapiens

Synonyms: C3orf11, FUS1, Fus-1 protein, Fusion 1 protein, LGCC, ...
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Disease relevance of TUSC2


Psychiatry related information on TUSC2

  • Less S-100 protein release was associated with better neuropsychological performance, as indexed by significant correlations with the Rey Auditory Verbal Learning memory test, descending Critical Flicker Fusion thresholds, and the Hospital Anxiety and Depression rating scales, typically around r=0 [5].
  • Performance on the Critical Flicker Fusion Frequency test, Choice Reaction Time, Immediate and Delayed Word Recall, and the Compensatory Tracking Task was significantly impaired by flurazepam but not by zolpidem-MR (with the exception of the Compensatory Tracking Task) or placebo [6].
  • Plasma triazolam and psychometric and memory tests (including Critical Flicker Fusion threshold, Choice Reaction Time, Digit Symbol Substitution and Self-Rating Scales) were assessed at regular intervals after the final treatment [7].
  • Psychomotor performance was measured using the following tests: Critical Flicker Fusion [8].
  • On the 1st and 3rd days of each of the three treatment periods subjects completed a battery of psychological tests including Critical Flicker Fusion (CFFT), Choice Reaction Time (CRT), tests of memory and subjective drug effects at 1, 2, 4 and 6 h after dosing [9].

High impact information on TUSC2

  • B43-PAP eliminated greater than 99.96% of blast progenitors under conditions in which only minimal inhibition of normal bone marrow progenitor cells (CFU-GM, CFU-E, CFU-MK, CFU-GEMM) was observed [10].
  • Pokeweed antiviral protein (PAP) from the summer leaves of Phytolacca americana was purified and conjugated via N-succinimidyl-3-(2-pyridyldithio)propionate to 9.2.27 anti-melanoma antibody to a glycoprotein-proteoglycan complex [11].
  • These results suggest that the 37,000-mol wt PAP is present only in certain cases of TTP, and is likely to be responsible for the formation of platelet thrombi in the microcirculation [12].
  • METHODS: Serum PAP was retrospectively monitored in 98 patients with acute pancreatitis during their stay in the hospital [13].
  • Retention of a Bean Phaseolin/Maize {gamma}-Zein Fusion in the Endoplasmic Reticulum Depends on Disulfide Bond Formation [14].

Chemical compound and disease context of TUSC2


Biological context of TUSC2

  • Other gene expression changes, including the increase of several apoptotic or anti-proliferation genes, such as GADD45A/B and TUSC2, and the decrease of a batch of phosphatase and kinase genes, may also provide further evidences in supporting the process of PSP induced apoptosis in cancer cells [20].
  • FUS1 is a novel tumor suppressor gene identified in the human chromosome 3p21.3 region that is deleted in many cancers [1].
  • Our results show that myristoylation is required for Fus1-mediated tumor-suppressing activity and suggest a novel mechanism for the inactivation of tumor suppressors in lung cancer and a role for deficient posttranslational modification in tumor suppressor-gene-mediated carcinogenesis [1].
  • In addition, we found no evidence for FUS1 promoter region methylation [2].
  • Here we report three PAP genes in the diploid Brassica rapa; the three PAPs are associated with different lipids in specific tissues [21].

Anatomical context of TUSC2

  • Loss of expression or a defect of myristoylation of the Fus1 protein was observed in human primary lung cancer and cancer cell lines [1].
  • In these organs PAP was localized in isolated plastid fractions [21].
  • In this work, we demonstrated that recombinant Vn50 bound P. rapae hemolymph components that were recognized by antisera to Tenebrio molitor prophenoloxidase (proPO) and Manduca sexta proPO-activating proteinase (PAP) [22].
  • Pokeweed antiviral protein (PAP), a 29-kD protein isolated from Phytolacca americana inhibits translation by catalytically removing a specific adenine residue from the large rRNA of the 60S subunit of eukaryotic ribosomes [23].
  • In vitro translation in the presence or absence of microsomal membranes shows that PAP is synthesized as a precursor and undergoes at least two different proteolytic processing steps to generate mature PAP [24].

Associations of TUSC2 with chemical compounds

  • This enzyme, designated prophenoloxidase-activating proteinase-2 (PAP-2), differs from another PAP, previously isolated from integuments of the same insect (PAP-1) [25].
  • The PAP cDNA was placed under control of the galactose-inducible GAL1 promoter and transformed into Saccharomyces cerevisiae [24].
  • Although GnRH-PAP conjugate protein bound specifically to and caused cell death in cells bearing the gonadotropin-releasing hormone (GnRH) receptor, we could not detect binding or cytotoxicity using two different versions of the fusion protein in receptor-positive cells [26].
  • By comparison, alanine substitutions of residues (28)KD(29), (80)FE(81), (111)SR(112), (166)FL(167) that are distant from the active site did not significantly reduce the enzymatic activity of PAP [27].
  • The Inhibitor of Apoptosis Protein Fusion c-IAP2{middle dot}MALT1 Stimulates NF-{kappa}B Activation Independently of TRAF1 AND TRAF2 [28].
  • Co-expression of FUS1 and c-ABL in COS1 cells blocked activation of c-Abl tyrosine kinase [29].

Regulatory relationships of TUSC2


Other interactions of TUSC2


Analytical, diagnostic and therapeutic context of TUSC2

  • Using surface-enhanced laser desorption/ionization mass spectrometric analysis on an anti-Fus1-antibody-capture ProteinChip array, we identified wild-type Fus1 as an N-myristoylated protein [1].
  • Studies using RT-PCR showed that in these latter species only totally spliced transcripts of PAP are present [36].
  • Gel filtration chromatography and native gel electrophoresis revealed the PAP-SPH, proPO-PAP, and SPH-proPO associations, essential for generating high Mr, active PO at the site of infection [37].
  • Circular dichroism, intrinsic fluorescence and chromatographic analysis of renaturating protein suggested that the kinetic intermediate of the hPAP folding is a monomer which displays a molten globule state (R. Kuciel, A. Mazurkiewicz & W.S. Ostrowski, 1996, Int. J. Biol. Macromol. 18, 167-175) [38].
  • Using fluorescence in situ hybridization, we determined that the three rat PAP genes, and the related REG gene map in the same chromosomes region, namely 4q33-->q34 [39].


  1. Myristoylation of the fus1 protein is required for tumor suppression in human lung cancer cells. Uno, F., Sasaki, J., Nishizaki, M., Carboni, G., Xu, K., Atkinson, E.N., Kondo, M., Minna, J.D., Roth, J.A., Ji, L. Cancer Res. (2004) [Pubmed]
  2. Overexpression of candidate tumor suppressor gene FUS1 isolated from the 3p21.3 homozygous deletion region leads to G1 arrest and growth inhibition of lung cancer cells. Kondo, M., Ji, L., Kamibayashi, C., Tomizawa, Y., Randle, D., Sekido, Y., Yokota, J., Kashuba, V., Zabarovsky, E., Kuzmin, I., Lerman, M., Roth, J., Minna, J.D. Oncogene (2001) [Pubmed]
  3. Human pulmonary alveolar proteinosis associated with a defect in GM-CSF/IL-3/IL-5 receptor common beta chain expression. Dirksen, U., Nishinakamura, R., Groneck, P., Hattenhorst, U., Nogee, L., Murray, R., Burdach, S. J. Clin. Invest. (1997) [Pubmed]
  4. Loss and reduction of FUS1 protein expression is a frequent phenomenon in the pathogenesis of lung cancer. Prudkin, L., Behrens, C., Liu, D.D., Zhou, X., Ozburn, N.C., Bekele, B.N., Minna, J.D., Moran, C., Roth, J.A., Ji, L., Wistuba, I.I. Clin. Cancer Res. (2008) [Pubmed]
  5. Neuropsychological change and S-100 protein release in 130 unselected patients undergoing cardiac surgery. Kilminster, S., Treasure, T., McMillan, T., Holt, D.W. Stroke (1999) [Pubmed]
  6. A double-blind, placebo- and flurazepam-controlled investigation of the residual psychomotor and cognitive effects of modified release zolpidem in young healthy volunteers. Blin, O., Micallef, J., Audebert, C., Legangneux, E. Journal of clinical psychopharmacology. (2006) [Pubmed]
  7. Troleandomycin-triazolam interaction in healthy volunteers: pharmacokinetic and psychometric evaluation. Warot, D., Bergougnan, L., Lamiable, D., Berlin, I., Bensimon, G., Danjou, P., Puech, A.J. Eur. J. Clin. Pharmacol. (1987) [Pubmed]
  8. Effects of single dose of gamma-hydroxybutyric acid and lorazepam on psychomotor performance and subjective feelings in healthy volunteers. Ferrara, S.D., Giorgetti, R., Zancaner, S., Orlando, R., Tagliabracci, A., Cavarzeran, F., Palatini, P. Eur. J. Clin. Pharmacol. (1999) [Pubmed]
  9. Psychopharmacological effects of pyritinol in normal volunteers. Hindmarch, I., Coleston, D.M., Kerr, J.S. Neuropsychobiology (1990) [Pubmed]
  10. Use of a novel colony assay to evaluate the cytotoxicity of an immunotoxin containing pokeweed antiviral protein against blast progenitor cells freshly obtained from patients with common B-lineage acute lymphoblastic leukemia. Uckun, F.M., Gajl-Peczalska, K.J., Kersey, J.H., Houston, L.L., Vallera, D.A. J. Exp. Med. (1986) [Pubmed]
  11. Immunotoxins to a human melanoma-associated antigen: resistance to pokeweed antiviral protein conjugates in vitro. Morgan, A.C., Bordonaro, J., Pearson, J.W., Sivam, G. J. Natl. Cancer Inst. (1987) [Pubmed]
  12. Novel platelet-agglutinating protein from a thrombotic thrombocytopenic purpura plasma. Siddiqui, F.A., Lian, E.C. J. Clin. Invest. (1985) [Pubmed]
  13. Serum levels of pancreatitis-associated protein as indicators of the course of acute pancreatitis. Multicentric Study Group on Acute Pancreatitis. Iovanna, J.L., Keim, V., Nordback, I., Montalto, G., Camarena, J., Letoublon, C., Lévy, P., Berthézène, P., Dagorn, J.C. Gastroenterology (1994) [Pubmed]
  14. Retention of a Bean Phaseolin/Maize {gamma}-Zein Fusion in the Endoplasmic Reticulum Depends on Disulfide Bond Formation. Pompa, A., Vitale, A. Plant Cell (2006) [Pubmed]
  15. Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell Fusion. Structure-function study. Kliger, Y., Aharoni, A., Rapaport, D., Jones, P., Blumenthal, R., Shai, Y. J. Biol. Chem. (1997) [Pubmed]
  16. Serum cholestenoic acid as a potential marker of pulmonary cholesterol homeostasis: increased levels in patients with pulmonary alveolar proteinosis. Meaney, S., Bonfield, T.L., Hansson, M., Babiker, A., Kavuru, M.S., Thomassen, M.J. J. Lipid Res. (2004) [Pubmed]
  17. Phosphorothioate Oligonucleotides Inhibit Human Immunodeficiency Virus Type 1 Fusion by Blocking gp41 Core Formation. Vaillant, A., Juteau, J.M., Lu, H., Liu, S., Lackman-Smith, C., Ptak, R., Jiang, S. Antimicrob. Agents Chemother. (2006) [Pubmed]
  18. Regulation of the avidity of ternary complexes containing the human 5-HT(1A) receptor by mutation of a receptor contact site on the interacting G protein alpha subunit. Welsby, P.J., Carr, I.C., Wilkinson, G., Milligan, G. Br. J. Pharmacol. (2002) [Pubmed]
  19. Deguanylation of human immunodeficiency virus (HIV-1) RNA by recombinant pokeweed antiviral protein. Rajamohan, F., Kurinov, I.V., Venkatachalam, T.K., Uckun, F.M. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  20. Molecular characterization of Coriolus versicolor PSP-induced apoptosis in human promyelotic leukemic HL-60 cells using cDNA microarray. Zeng, F., Hon, C.C., Sit, W.H., Chow, K.Y., Hui, R.K., Law, I.K., Ng, V.W., Yang, X.T., Leung, F.C., Wan, J.M. Int. J. Oncol. (2005) [Pubmed]
  21. Brassica rapa has three genes that encode proteins associated with different neutral lipids in plastids of specific tissues. Kim, H.U., Wu, S.S., Ratnayake, C., Huang, A.H. Plant Physiol. (2001) [Pubmed]
  22. Negative regulation of prophenoloxidase (proPO) activation by a clip-domain serine proteinase homolog (SPH) from endoparasitoid venom. Zhang, G., Lu, Z.Q., Jiang, H., Asgari, S. Insect Biochem. Mol. Biol. (2004) [Pubmed]
  23. Plant resistance to fungal infection induced by nontoxic pokeweed antiviral protein mutants. Zoubenko, O., Uckun, F., Hur, Y., Chet, I., Tumer, N. Nat. Biotechnol. (1997) [Pubmed]
  24. Isolation and characterization of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: identification of residues important for toxicity. Hur, Y., Hwang, D.J., Zoubenko, O., Coetzer, C., Uckun, F.M., Tumer, N.E. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  25. Prophenoloxidase-activating proteinase-2 from hemolymph of Manduca sexta. A bacteria-inducible serine proteinase containing two clip domains. Jiang, H., Wang, Y., Yu, X.Q., Kanost, M.R. J. Biol. Chem. (2003) [Pubmed]
  26. Binding and cytotoxicity of conjugated and recombinant fusion proteins targeted to the gonadotropin-releasing hormone receptor. Qi, L., Nett, T.M., Allen, M.C., Sha, X., Harrison, G.S., Frederick, B.A., Crawford, E.D., Glode, L.M. Cancer Res. (2004) [Pubmed]
  27. Modeling and alanine scanning mutagenesis studies of recombinant pokeweed antiviral protein. Rajamohan, F., Pugmire, M.J., Kurinov, I.V., Uckun, F.M. J. Biol. Chem. (2000) [Pubmed]
  28. The Inhibitor of Apoptosis Protein Fusion c-IAP2{middle dot}MALT1 Stimulates NF-{kappa}B Activation Independently of TRAF1 AND TRAF2. Varfolomeev, E., Wayson, S.M., Dixit, V.M., Fairbrother, W.J., Vucic, D. J. Biol. Chem. (2006) [Pubmed]
  29. Oncogenic activation of c-Abl in non-small cell lung cancer cells lacking FUS1 expression: inhibition of c-Abl by the tumor suppressor gene product Fus1. Lin, J., Sun, T., Ji, L., Deng, W., Roth, J., Minna, J., Arlinghaus, R. Oncogene (2007) [Pubmed]
  30. Tetraspanins CD9 and CD81 Modulate HIV-1-Induced Membrane Fusion. Gord??n-Alonso, M., Ya??ez-M??, M., Barreiro, O., Alvarez, S., Mu??oz-Fern??ndez, M.A., Valenzuela-Fern??ndez, A., S??nchez-Madrid, F. J. Immunol. (2006) [Pubmed]
  31. A Second SNARE Role for Exocytic SNAP25 in Endosome Fusion. Aikawa, Y., Lynch, K.L., Boswell, K.L., Martin, T.F. Mol. Biol. Cell (2006) [Pubmed]
  32. DC-SIGN Facilitates Fusion of Dendritic Cells with Human T-Cell Leukemia Virus Type 1-Infected Cells. Ceccaldi, P.E., Delebecque, F., Prevost, M.C., Moris, A., Abastado, J.P., Gessain, A., Schwartz, O., Ozden, S. J. Virol. (2006) [Pubmed]
  33. Functional characterization of the 5' flanking region of human ubiquitin fusion degradation 1 like gene (UFD1L). Amati, F., Conti, E., Botta, A., Amicucci, P., Dallapiccola, B., Novelli, G. Cell Biochem. Funct. (2002) [Pubmed]
  34. Expression of Variant TMPRSS2/ERG Fusion Messenger RNAs Is Associated with Aggressive Prostate Cancer. Wang, J., Cai, Y., Ren, C., Ittmann, M. Cancer Res. (2006) [Pubmed]
  35. Insulin Signaling Diverges into Akt-dependent and -independent Signals to Regulate the Recruitment/Docking and the Fusion of GLUT4 Vesicles to the Plasma Membrane. Gonzalez, E., McGraw, T.E. Mol. Biol. Cell (2006) [Pubmed]
  36. Identification of a short interspersed repetitive element in partially spliced transcripts of the bell pepper (Capsicum annuum) PAP gene: new evolutionary and regulatory aspects on plant tRNA-related SINEs. Pozueta-Romero, J., Houlné, G., Schantz, R. Gene (1998) [Pubmed]
  37. Manduca sexta prophenoloxidase (proPO) activation requires proPO-activating proteinase (PAP) and serine proteinase homologs (SPHs) simultaneously. Gupta, S., Wang, Y., Jiang, H. Insect Biochem. Mol. Biol. (2005) [Pubmed]
  38. Molten globule as an intermediate on the human prostatic phosphatase folding pathway. Kuciel, R., Mazurkiewicz, A. Acta Biochim. Pol. (1997) [Pubmed]
  39. The rat genes encoding the pancreatitis-associated proteins I, II and III (Pap1, Pap2, Pap3), and the lithostathin/pancreatic stone protein/regeneration protein (Reg) colocalize at 4q33-->q34. Stephanova, E., Tissir, F., Dusetti, N., Iovanna, J., Szpirer, J., Szpirer, C. Cytogenet. Cell Genet. (1996) [Pubmed]
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