The Mad2 spindle checkpoint protein has two distinct natively folded states (original) (raw)
References
Nasmyth, K. Segregating sister genomes: the molecular biology of chromosome separation. Science297, 559–565 (2002). ArticleCAS Google Scholar
Cleveland, D.W., Mao, Y. & Sullivan, K.F. Centromeres and kinetochores. From epigenetics to mitotic checkpoint signaling. Cell112, 407–421 (2003). ArticleCAS Google Scholar
Yu, H. Regulation of APC-Cdc20 by the spindle checkpoint. Curr. Opin. Cell Biol.14, 706–714 (2002). ArticleCAS Google Scholar
Shah, J.V. & Cleveland, D.W. Waiting for anaphase: Mad2 and the spindle assembly checkpoint. Cell103, 997–1000 (2000). ArticleCAS Google Scholar
Tang, Z., Bharadwaj, R., Li, B. & Yu, H. Mad2-independent inhibition of APCCdc20 by the mitotic checkpoint protein BubR1. Dev. Cell1, 227–237 (2001). ArticleCAS Google Scholar
Sudakin, V., Chan, G.K. & Yen, T.J. Checkpoint inhibition of the APC/C in HeLa cells is mediated by a complex of BUBR1, BUB3, CDC20, and MAD2. J. Cell Biol.154, 925–936 (2001). ArticleCAS Google Scholar
Fang, G. Checkpoint protein BubR1 acts synergistically with Mad2 to inhibit anaphase-promoting complex. Mol. Biol. Cell13, 755–766 (2002). ArticleCAS Google Scholar
Chen, R.H. BubR1 is essential for kinetochore localization of other spindle checkpoint proteins and its phosphorylation requires Mad1. J. Cell Biol.158, 487–496 (2002). ArticleCAS Google Scholar
Millband, D.N. & Hardwick, K.G. Fission yeast Mad3p is required for Mad2p to inhibit the anaphase-promoting complex and localizes to kinetochores in a Bub1p-, Bub3p-, and Mph1p-dependent manner. Mol. Cell. Biol.22, 2728–2742 (2002). ArticleCAS Google Scholar
Chen, R.H., Brady, D.M., Smith, D., Murray, A.W. & Hardwick, K.G. The spindle checkpoint of budding yeast depends on a tight complex between the Mad1 and Mad2 proteins. Mol. Biol. Cell10, 2607–2618 (1999). ArticleCAS Google Scholar
Luo, X., Tang, Z., Rizo, J. & Yu, H. The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20. Mol. Cell9, 59–71 (2002). Article Google Scholar
Chung, E. & Chen, R.H. Spindle checkpoint requires Mad1-bound and Mad1-free Mad2. Mol. Biol. Cell13, 1501–1511 (2002). ArticleCAS Google Scholar
Habu, T., Kim, S.H., Weinstein, J. & Matsumoto, T. Identification of a MAD2-binding protein, CMT2, and its role in mitosis. EMBO J.21, 6419–6428 (2002). ArticleCAS Google Scholar
Wassmann, K., Liberal, V. & Benezra, R. Mad2 phosphorylation regulates its association with Mad1 and the APC/C. EMBO J.22, 797–806 (2003). ArticleCAS Google Scholar
Sironi, L. et al. Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint. EMBO J.21, 2496–2506 (2002). ArticleCAS Google Scholar
Luo, X. et al. Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20. Nat. Struct. Biol.7, 224–229 (2000). ArticleCAS Google Scholar
Musacchio, A. & Hardwick, K.G. The spindle checkpoint: structural insights into dynamic signaling. Nat. Rev. Mol. Cell Biol.3, 731–741 (2002). ArticleCAS Google Scholar
Sironi, L. et al. Mad2 binding to Mad1 and Cdc20, rather than oligomerization, is required for the spindle checkpoint. EMBO J.20, 6371–6382 (2001). ArticleCAS Google Scholar
Fang, G., Yu, H. & Kirschner, M.W. The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation. Genes Dev.12, 1871–1883 (1998). ArticleCAS Google Scholar
Canman, J.C., Salmon, E.D. & Fang, G. Inducing precocious anaphase in cultured mammalian cells. Cell Motil. Cytoskeleton52, 61–65 (2002). Article Google Scholar
Altmann, F., Staudacher, E., Wilson, I.B. & Marz, L. Insect cells as hosts for the expression of recombinant glycoproteins. Glycoconj. J.16, 109–123 (1999). ArticleCAS Google Scholar
Dhalluin, C. et al. Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors. Mol. Cell6, 921–929 (2000). ArticleCAS Google Scholar
Bullough, P.A., Hughson, F.M., Skehel, J.J. & Wiley, D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature371, 37–43 (1994). ArticleCAS Google Scholar
Sauter, N.K., Mau, T., Rader, S.D. & Agard, D.A. Structure of α-lytic protease complexed with its pro region. Nat. Struct. Biol.5, 945–950 (1998). ArticleCAS Google Scholar
Barrientos, L.G. et al. The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures. Structure10, 673–686 (2002). ArticleCAS Google Scholar
Khazanovich, N., Bateman, K., Chernaia, M., Michalak, M. & James, M. Crystal structure of the yeast cell-cycle control protein, p13suc1, in a strand-exchanged dimer. Structure4, 299–309 (1996). ArticleCAS Google Scholar
Ye, S. & Goldsmith, E.J. Serpins and other covalent protease inhibitors. Curr. Opin. Struct. Biol.11, 740–745 (2001). ArticleCAS Google Scholar
Volkman, B.F., Lipson, D., Wemmer, D.E. & Kern, D. Two-state allosteric behavior in a single-domain signaling protein. Science291, 2429–2433 (2001). ArticleCAS Google Scholar
James, L.C., Roversi, P. & Tawfik, D.S. Antibody multispecificity mediated by conformational diversity. Science299, 1362–1367 (2003). ArticleCAS Google Scholar
Mottonen, J. et al. Structural basis of latency in plasminogen activator inhibitor-1. Nature355, 270–273 (1992). ArticleCAS Google Scholar
Howell, B.J., Hoffman, D.B., Fang, G., Murray, A.W. & Salmon, E.D. Visualization of Mad2 dynamics at kinetochores, along spindle fibers, and at spindle poles in living cells. J. Cell Biol.150, 1233–1250 (2000). ArticleCAS Google Scholar
Hardwick, K.G., Weiss, E., Luca, F.C., Winey, M. & Murray, A.W. Activation of the budding yeast spindle assembly checkpoint without mitotic spindle disruption. Science273, 953–956 (1996). ArticleCAS Google Scholar
Seeley, T.W., Wang, L. & Zhen, J.Y. Phosphorylation of human MAD1 by the BUB1 kinase in vitro . Biochem. Biophys. Res. Commun.257, 589–595 (1999). ArticleCAS Google Scholar
Clore, G.M. & Gronenborn, A.M. NMR structure determination of proteins and protein complexes larger than 20 kDa. Curr. Opin. Chem. Biol.2, 564–570 (1998). ArticleCAS Google Scholar
Gardner, K.H. & Kay, L.E. The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct.27, 357–406 (1998). ArticleCAS Google Scholar
Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR13, 289–302 (1999). ArticleCAS Google Scholar
Brünger, A.T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D54, 905–921 (1998). Article Google Scholar
Elbashir, S.M. et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature411, 494–498 (2001). ArticleCAS Google Scholar
Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr.24, 946–950 (1991). Article Google Scholar
Kuzmic, P. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV Proteinase. Anal. Biochem.237, 260–273 (1996). ArticleCAS Google Scholar