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GTP Binding Is Required for SEPT12 to Form Filaments and to Interact with SEPT11  

Ding, Xiangming (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University)
Yu, Wenbo (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University)
Liu, Ming (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University)
Shen, ShuQing (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University)
Chen, Fang (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University)
Cao, Lihuan (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University)
Wan, Bo (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University)
Yu, Long (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University)
Publication Information
Molecules and Cells / v.25, no.3, 2008 , pp. 385-389 More about this Journal
Abstract
Septins are a family of filament-forming GTP-binding proteins involved in a variety of cellular process such as cytokinesis, exocytosis, and membrane dynamics. Here we report the biochemical and immunocytochemical characterization of a recently identified mammalian septin, SEPT12. SEPT12 binds GTP in vitro, and a mutation (Gly56 to Asn) in the GTP-binding motif abolished binding. Immunocytochemical analysis revealed that wild-type SEPT12 formed filamentous structures when transiently expressed in Hela cells whereas $SEPT12^{G56A}$ generated large aggregates. In addition, wild-type SEPT12 failed to form filaments when coexpressed with $SEPT12^{G56A}$. We also observed that GTP-binding by SEPT12 is required for interaction with SEPT11 but not with itself.
Keywords
Co-localization; GTP-binding Domain; Protein Interaction; Septin; Subcellular Localization;
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1 Blaser, S., Horn, J., Wurmell, P., Bauer, H., Strumpell, S., Nurden, P., Pagenstecher, A., Busse, A., Wunderle, D., Hainmann, I., et al. (2004). The novel human platelet septin SEPT8 is an interaction partner of SEPT4. Thromb. Haemost. 91, 959-966
2 Field, C.M., and Kellogg, D. (1999). Septins: cytoskeletal polymers or signalling GTPases? Trends Cell Biol. 9, 387-394   DOI   ScienceOn
3 Ihara, M., Tomimoto, H., Kitayama, H., Morioka, Y., Akiguchi, I., Shibasaki, H., Noda, M., and Kinoshita, M. (2003). Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies. J. Biol. Chem. 278, 24095-24102   DOI   ScienceOn
4 Kinoshita, M. (2003). Assembly of mammalian septins. J. Biochem. (Tokyo). 134, 491-496   DOI   ScienceOn
5 McIlhatton, M.A., Burrows, J.F., Donaghy, P.G., Chanduloy, S., Johnston, P.G., and Russell, S.E. (2001). Genomic organization, complex splicing pattern and expression of a human septin gene on chromosome 17q25.3. Oncogene 20, 5930-5939   DOI
6 Versele, M., and Thorner, J. (2005). Some assembly required: yeast septins provide the instruction manual. Trends Cell Biol. 15, 414-424   DOI   ScienceOn
7 Beites, C.L., Xie, H., Bowser, R., and Trimble, W.S. (1999). The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nat. Neurosci. 2, 434-439   DOI   ScienceOn
8 Kinoshita, M., Field, C.M., Coughlin, M.L., Straight, A.F., and Mitchison, T.J. (2002). Self- and actin-templated assembly of Mammalian septins. Dev. Cell. 3, 791-802   DOI   ScienceOn
9 Mendoza, M., Hyman, A.A., and Glotzer, M. (2002). GTP binding induces filament assembly of a recombinant septin. Curr. Biol. 12, 1858-1863   DOI   ScienceOn
10 Nagata, K., Kawajiri, A., Matsui, S., Takagishi, M., Shiromizu, T., Saitoh, N., Izawa, I., Kiyono, T., Itoh, T.J., Hotani, H., et al. (2003). Filament formation of MSF-A, a mammalian septin, in human mammary epithelial cells depends on interactions with microtubules. J. Biol. Chem. 278, 18538-18543   DOI   ScienceOn
11 Cooper, J.A., and Kiehart, D.P. (1996). Septins may form a ubiquitous family of cytoskeletal filaments. J. Cell Biol. 134, 1345-1348   DOI
12 Kinoshita, M., Kumar, S., Mizoguchi, A., Ide, C., Kinoshita, A., Haraguchi, T., Hiraoka, Y., and Noda, M. (1997). Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures. Genes Dev. 11, 1535-1547   DOI   ScienceOn
13 Russell, S.E., and Hall, P.A. (2005). Do septins have a role in cancer? Br. J. Cancer. 93, 499-503   DOI   ScienceOn
14 Xue, J., Wang, X., Malladi, C.S., Kinoshita, M., Milburn, P.J., Lengyel, I., Rostas, J.A., and Robinson, P.J. (2000). Phosphorylation of a new brain-specific septin, G-septin, by cGMP-dependent protein kinase. J. Biol. Chem. 275, 10047-10056   DOI   ScienceOn
15 Adam, J.C., Pringle, J.R., and Peifer, M. (2000). Evidence for functional differentiation among Drosophila septins in cytokinesis and cellularization. Mol. Biol. Cell. 11, 3123-3135   DOI
16 Vrabioiu, A.M., Gerber, S.A., Gygi, S.P., Field, C.M., and Mitchison, T.J. (2004). The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides. J. Biol. Chem. 279, 3111-3118   DOI   ScienceOn
17 Hall, P.A., Jung, K., Hillan, K.J., and Russell, S.E. (2005). Expression profiling the human septin gene family. J. Pathol. 206, 269-278   DOI   ScienceOn
18 Surka, M.C., Tsang, C.W., and Trimble, W.S. (2002). The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis. Mol. Biol. Cell 13, 3532-3545   DOI   ScienceOn
19 Nagata, K., Asano, T., Nozawa, Y., and Inagaki, M. (2004). Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11. J. Biol. Chem. 279, 55895-55904   DOI   ScienceOn
20 Hanai, N., Nagata, K., Kawajiri, A., Shiromizu, T., Saitoh, N., Hasegawa, Y., Murakami, S., and Inagaki, M. (2004). Biochemical and cell biological characterization of a mammalian septin, Sept11. FEBS Lett. 568, 83-88   DOI   ScienceOn
21 Hsu, S.C., Hazuka, C.D., Roth, R., Foletti, D.L., Heuser, J., and Scheller, R.H. (1998). Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron 20, 1111-1122   DOI   ScienceOn
22 Hartwell, L.H. (1971). Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis. Exp. Cell Res. 69, 265-276   DOI   ScienceOn
23 Martinez, C., Sanjuan, M.A., Dent, J.A., Karlsson, L., and Ware, J. (2004). Human septin-septin interactions as a prerequisite for targeting septin complexes in the cytosol. Biochem. J. 382, 783-791   DOI   ScienceOn
24 Blaser, S., Roseler, S., Rempp, H., Bartsch, I., Bauer, H., Lieber, M., Lessmann, E., Weingarten, L., Busse, A., Huber, M., et al. (2006). Human endothelial cell septins: SEPT11 is an interaction partner of SEPT5. J. Pathol. 210, 103-110   DOI   ScienceOn
25 Versele, M., and Thorner, J. (2004). Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4. J. Cell Biol. 164, 701-715   DOI   ScienceOn
26 Field, C.M., al-Awar, O., Rosenblatt, J., Wong, M.L., Alberts, B., and Mitchison, T.J. (1996). A purified Drosophila septin complex forms filaments and exhibits GTPase activity. J. Cell Biol. 133, 605-616   DOI   ScienceOn
27 Larisch, S., Yi, Y., Lotan, R., Kerner, H., Eimerl, S., Tony Parks, W., Gottfried, Y., Birkey, Reffey S., de Caestecker, M.P., Danielpour, D., et al. (2000). A novel mitochondrial septinlike protein, ARTS, mediates apoptosis dependent on its Ploop motif. Nat. Cell Biol. 2, 915-921   DOI   ScienceOn