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Research

Cell Cycle and Cell Proliferation

at the Biocenter, Area Biochemistry and Chemistry, Innsbruck
Research Leader: Dr. Ludger Hengst 

Publications:

  • Grimmler, M., Wang, Y., Mund, T., Cilensek, Z., Keidel, E.M., Waddell, M.B., Jäckel, H., Kullmann, M., Kriwacki, R.W. and Hengst, L. (2007). The Cdk-inhibitory activity and stability of
    p27Kip1 are directly regulated by oncogenic tyrosine kinases. Cell, 128, 269 - 280.
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  • Chu, I.M.; Sun, J., Arnaout, A, Kahn, H., Hanna, W., Narod, S., Sun, P., Keat-Tan, C.; Hengst, L. and Slingerland J. M. (2007). p27 phosphorylation by Src regulates inhibition of Cyclin E / Cdk2 and p27 proteolysis. Cell, 128, 281-294.
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  • Schmees, C, Prinz, C, Treptau, T., Rad, R., Hengst, L., Voland, P., Bauer, S., Brenner, L., Schmid, R. M. and Gerhard, M. (2007). Inhibition of T cell proliferation by Helicobacter pylori γ-glutamyl transpeptidase. Gastroenterology, 132, 1820 - 1833.
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  • Geley, S. and Hengst, L. (2008). Zellzyklus und Spindelapparat. In: Die Onkologie. 2. Auflage. W. Hiddemann, Bartram C. R. (Eds.). Springer Verlag. In press.
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  • Halfter, H.,  Friedrich, M.,  Resch, A.,  Kullmann, M., Stögbauer, F.,  Ringelstein, E.B. and Hengst, L. (2006). Oncostatin M induces growth arrest by inhibition of Skp2, Cks1, and cyclin A expression and induced p21 expression.  Cancer Research 66, 6530-6539.
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  • Hengst, L. and Nigg, E.A. (2006). Cell cycle – An overview. Encyclopedic Reference of Genomics and Proteomics in Molecular Medicine. D. Ganten und K. Ruckpaul (Eds.). Springer Verlag 2006.
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  • Jaschke, B., Michaelis, C., Milz, S., Vogeser, M., Mund, T., Hengst, L., Kastrati, A., Schömig, A., Wessely, R. (2005). Local statin therapy differentially interferes with smooth muscle and endothelial cell proliferation and reduces neointima on a drug-eluting stent platform. Cardiovasc Res. 68, 483-492.
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  • Gerhard, M., Schmees, C., Voland, P.,  Endres, N., , Sander,M., Reindl, W., Rad, R., Oelsner, M., Decker,T., Mempel, M., Hengst, L. and Prinz, C. (2005). A secreted low molecular weight protein from Helicobacter pylori induces cell cycle arrest of T-cells. Gastroenterology 128, 1327-1339.
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  • Swaminathan, S., Körner, R., Kiendl, F., Luptti, R., Hengst, L. and Melchior, F. (2004). RanGAP*SUMO-1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly. Journal of Cell Biology 164, 965-971.
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  • Lacy, E.R., Filippov, I., Otieno, S., Xiao, L., Lewis, W.S., Sivakolundu, S., Weiss, S., Hengst, L. and Kriwacki, R.W. (2004). p27 Binds Cyclin/Cyclin-dependent Kinase Complexes via a Sequential Mechanism involving Binding-induced Protein Folding. Nature Structural & Molecular Biology 11, 358-364.
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  • Hengst, L. (2004). A second RING to destroy p27Kip1. Nature Cell Biology, 6, 1153-1155.
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  • Pendergraft III, W.F., Rudolph, E.H., Grimmler, M., Hengst, L., Falk,R.J., Jennette, J.C.  and Preston, G. A. . (2004). Proteinase 3 sidesteps caspases and cleaves p21Waf1/Cip1/Sdi to induce endothelial cell apoptosis. Kidney International 65, 75-84.
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  • Göpfert, U. , Kullmann, M. and Hengst, L (2003). Cell Cycle dependent translation of p27 involves a responsive element in its 5’UTR that overlaps with an uORF. Human Molecular Genetics 12. 1767-1779.
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  • Connor, M.K., Kotchetkov, R., Cariou, S., Beniston, R.G., Resch, A., Lupetti, R., Melchior, F., Hengst, L.*,  and Slingerland, J.M.* (2003). *Communicating authors.CRM1/Ran-mediated nuclear export of p27Kip1 involves a nuclear export signal and links p27 export and proteolysis. Molecular Biology of the Cell 14. 201-213.
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  • Wessely, R., Hengst, L., Wegener, F.,  Richter, T., Paskalidis, M., Schomig, A., Brandl, R., Neumann, F.J.(2003).  IRF-1 is essential for the limitation of neointima hyperplasia: Implications for the pathophysiology of neointima formation and therapeutic prevention of restenotic lesions following coronary angioplasty. Human Molecular Genetics, 12. 177-187.
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  • Kullmann M., Göpfert, U., Siewe, B. and Hengst, L. (2002).  ELAV/Hu proteins inhibit p27 translation through an IRES element in the p27 5'UTR. Genes & Development 16, 3087-3099.
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  • Melchior, F. and Hengst, L. (2002). Sumo1-p53. Cell Cycle 1, 245-249.
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  • Melchior, F and Hengst, L. (2000).  Mdm2-SUMO1: Is bigger better?  Nature Cell Biology 2, E161-E163.
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  • Hengst, L., Göpfert, U.,  Lashuel, H. A. and Reed, S.I. (1998). Complete inhibition of Cdk/Cyclin by one molecule of p21Cip1. Genes & Development 12, 3882-3888.
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  • Hengst, L. and Reed, S.I. (1998). Inhibitors of the Cip/Kip Family.  Current Topics in Microbiology and Immunology, 227. 25-41
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  • Niculescu III, A., Chen, X., Smeets, M., Hengst, L., Prives, C. and Reed, S. I. (1998). Effects of p21Cip1/Waf1 on both the G1/S and the G2/M cell cycle transitions: pRb as a critical determinant in blocking and in preventing endoreduplication. Mol. Cell. Biol., 18.  629-643.
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  • Kiwacki, R.W., Hengst, L., Tennant, L., Reed, S.I. and Wright, P. E. (1996). Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2 bound state: conformational disorder mediates binding diversity. PNAS, 93. 11504-11509.
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  • Hengst, L. and Reed, S.I. (1996). Translational control of p27Kip1 accumulation during the cell cycle. Science, 271. 1861-1864.
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  • Hengst, L., Grabowski, R.  and Gallwitz, D.(1996).  Ypt6. In: Guidebook to the small GTPases. M. Zerial und L.A. Huber. Oxford University Press.
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  • Hengst, L. and Gallwitz, D. (1996). Ryh1. In: Guidebook to the small GTPases. M. Zerial und L.A. Huber. Oxford University Press.
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  • Resnitzky, D., Hengst, L. and Reed, S.I.R. (1995). Cyclin A associated kinase activity is rate-limiting for entrance into S phase, and is negatively regulated in G1 by p27Kip1.  Mol Cell Biol., 15 . 4347-4352.
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  • Reed, S.I., Bailly, E., Dulic, V., Hengst, L., Resnitzky, D., and Slingerland, J. (1994). G1 control in mammalian cells. J. Cell Sci. - Suppl.18: 69-73.
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  • Slingerland, J.M., Hengst, L., Alexander, D., Stampfer, M.R. and Reed, S.I. (1994). A novel inhibitor of Cyclin/Cdk activity detected in transforming growth factor -arrested epithelial cells. Mol. Cell. Biol., 14: 3683-3694.
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  • Hengst, L., Dulic, V,. Slingerland, JM., Lees, E. and Reed SI. (1994). A cell cycle-regulated inhibitor of cyclin-dependent kinases. PNAS, 91. 5291-5295.
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  • Kibbe, W., Hengst, L. and Gallwitz, D. (1993). The Ypt Gene family in yeast. In: The ras superfamily of GTPases. Edited by F. McCormick and J.C. Lacal. CRC Press Inc.
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  • Bednarek S. Y.,  Reynolds T. L.,  Schroeder M.,  Grabowski R.,  Hengst L., Gallwitz D.  and Raikhel, N.V. (1994). A small GTP-binding protein from Arabidopsis thaliana functionally complements the yeast YPT6 null mutant. Plant Physiol.  104 : 591-596
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  • Wichmann, H., Hengst, L., Gallwitz, D., Schimmoeller, F. and Riezman, H. (1994). YPT7. In: Rothblatt, J., Novick, P., Stevens, T.H.: Guidebook to the secretory pathway. 272 Oxford University Press.
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  • Wichmann, H., Hengst, L. and Gallwitz, D. (1992). Endocytosis in yeast: Evidence for the involvement of a small GTP-binding protein (Ypt7p). Cell 71, 1131-1142.
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  • Wagner, P., Hengst, L. and Gallwitz, D. (1992). Ypt proteins in yeast. Methods Enzymol., 219, 369-387.
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  • Gallwitz, D., Becker, J., Benli, M., Hengst, L., Morsin-Huaman, C., Tan, J., Vollmer, P. and Wichman, H. (1991). The YPT-branch of the ras superfamily in yeast: functional importance of the putative effector region. In:  NATO ASI-Series, Plenum press, New York.
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  • Hengst, L., Lehmeier, T. and Gallwitz, D. (1990). The ryh1 gene in the fission yeast Schizosaccharomyces pombe encoding a GTP-binding protein related to ras, rho and ypt: structure, expression and identification of its human homologue. EMBO J., 9, 1949-1955.
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  • Kadenbach, B., Schlerf, A., Mengel, T., Hengst, L., Cao, X., Suske, G., Eckerskorn, C. and Lottspeich, F. (1989). Tissue-spezific expression of nuclear genes for mitochondrial enzymes. In: Organelles in eucaryotic cells. (eds: Tager, J.M.,  Azzi, A., Papa, S. and Guerrieri, F.). Plenum press, New York.
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  • Cao, X., Hengst, L., Schlerf, A., Droste, M., Mengel, T. and Kadenbach, B. (1988). Complexity of nuclear-encoded genes of mammalian cytochrom c oxidase. Ann. N.Y. Acad. Sci., 550, 337-347.

Biocenter, Area Biochemistry and Chemistry