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Gene Review

SEPT2  -  septin 2

Homo sapiens

Synonyms: DIFF6, KIAA0158, NEDD-5, NEDD5, Neural precursor cell expressed developmentally down-regulated protein 5, ...
 
 
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Disease relevance of SEPT2

  • We then characterized the expression and subcellular distribution of the SEPT2 protein in aphidicolin-synchronized U373 MG astrocytoma cells by immunofluorescence and fluorescence-activated cell sorter analysis [1].
  • SEPT2 was abundantly expressed in all brain tumor samples and cell lines studied [1].
  • SEPT2 is a new fusion partner of MLL in acute myeloid leukemia with t(2;11)(q37;q23) [2].
  • Furthermore, we found dysregulated expression of genes not previously associated with pancreatic adenocarcinoma, such as Rac 1, GLG1, NEDD5, RPL-13a, RPS9 and members of the Wnt5A gene family [3].
  • Proteomic identification of a role for the von Hippel Lindau tumour suppressor in changes in the expression of mitochondrial proteins and septin 2 in renal cell carcinoma [4].
 

High impact information on SEPT2

 

Biological context of SEPT2

 

Anatomical context of SEPT2

  • Extracellularly added calumenin decreases the levels of both the N-terminal and C-terminal actin fragments, and, in addition, decreases the expression level of septin 2, which interacts with the actin cytoskeleton and is involved in cytokinesis [8].
 

Associations of SEPT2 with chemical compounds

  • In addition, we show that recombinant septin 2 binds guanine nucleotides with a Kd of 0.28 microm for GTPgammaS and 1.75 microm for GDP [9].
 

Regulatory relationships of SEPT2

 

Other interactions of SEPT2

  • It is shown that SEPT13 and the other known human septins are expressed in all tissue types but some show high expression in lymphoid (SEPT1, 6, 9, and 12) or brain tissues (SEPT2, 3, 4, 5, 7, 8, and 11) [10].
  • Additional predictions with the motif scan programs Scansite and Prosite suggest that the phosphorylation of wild-type Sept2 might be a potential substrate for casein kinase 2 [11].
  • The location of phosphorylation in Sept2 differs from the sites predicted for cGMP-dependent protein kinase (PKG) phosphorylation in Septin 3, raising the possibility that different septins may undergo distinct phosphorylation events that could control their functions in important cellular processes such as neurotransmission or cytokinesis [11].
  • A cascade involving p85, Cdc42 and septin 2 regulates cytokinesis [12].

References

  1. Analysis of mammalian septin expression in human malignant brain tumors. Kim, D.S., Hubbard, S.L., Peraud, A., Salhia, B., Sakai, K., Rutka, J.T. Neoplasia (2004) [Pubmed]
  2. SEPT2 is a new fusion partner of MLL in acute myeloid leukemia with t(2;11)(q37;q23). Cerveira, N., Correia, C., Bizarro, S., Pinto, C., Lisboa, S., Mariz, J.M., Marques, M., Teixeira, M.R. Oncogene (2006) [Pubmed]
  3. Gene expression profiles of pancreatic cancer and stromal desmoplasia. Crnogorac-Jurcevic, T., Efthimiou, E., Capelli, P., Blaveri, E., Baron, A., Terris, B., Jones, M., Tyson, K., Bassi, C., Scarpa, A., Lemoine, N.R. Oncogene (2001) [Pubmed]
  4. Proteomic identification of a role for the von Hippel Lindau tumour suppressor in changes in the expression of mitochondrial proteins and septin 2 in renal cell carcinoma. Craven, R.A., Hanrahan, S., Totty, N., Harnden, P., Stanley, A.J., Maher, E.R., Harris, A.L., Trimble, W.S., Selby, P.J., Banks, R.E. Proteomics (2006) [Pubmed]
  5. A PI3K activity-independent function of p85 regulatory subunit in control of mammalian cytokinesis. Garc??a, Z., Silio, V., Marqu??s, M., Cort??s, I., Kumar, A., Hernandez, C., Checa, A.I., Serrano, A., Carrera, A.C. EMBO J. (2006) [Pubmed]
  6. Structural analysis of septin 2, 6, and 7 complexes. Low, C., Macara, I.G. J. Biol. Chem. (2006) [Pubmed]
  7. Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Kremer, B.E., Haystead, T., Macara, I.G. Mol. Biol. Cell (2005) [Pubmed]
  8. Proteomic profiling of fibroblasts reveals a modulating effect of extracellular calumenin on the organization of the actin cytoskeleton. Ostergaard, M., Hansen, G.A., Vorum, H., Honoré, B. Proteomics (2006) [Pubmed]
  9. GTP binding and hydrolysis kinetics of human septin 2. Huang, Y.W., Surka, M.C., Reynaud, D., Pace-Asciak, C., Trimble, W.S. FEBS J. (2006) [Pubmed]
  10. Expression profiling the human septin gene family. Hall, P.A., Jung, K., Hillan, K.J., Russell, S.E. J. Pathol. (2005) [Pubmed]
  11. Septin 2 phosphorylation: theoretical and mass spectrometric evidence for the existence of a single phosphorylation site in vivo. She, Y.M., Huang, Y.W., Zhang, L., Trimble, W.S. Rapid Commun. Mass Spectrom. (2004) [Pubmed]
  12. A cascade involving p85, Cdc42 and septin 2 regulates cytokinesis. Silió, V., Marqués, M., Cortés, I., Zuluaga, S., Carrera, A.C. Biochem. Soc. Trans. (2007) [Pubmed]
 
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