Poly(ADP-ribose) is required for spindle assembly and structure

Nature

Volumn 432, Issue 7017, 2004, Pages 645-649

  Chang, Paul ^a   Jacobson, Myron K ^b   Mitchison, Timothy J ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CELLS; CHROMOSOMES; DNA; HYDROLYSIS; LIPIDS; MACROMOLECULES; PERTURBATION TECHNIQUES; POLYMERIZATION;

MICROTUBULES; MITOTIC SPINDLES; SPINDLE COMPONENTS;

PROTEINS;

DNA; LIPID; MICROTUBULE ASSOCIATED PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; POLY(ADENOSINE DIPHOSPHATE RIBOSE); PROTEIN; RNA;

BIOLOGY;

ARTICLE; CHROMOSOME SEGREGATION; DYNAMICS; MACROMOLECULE; MICROTUBULE; MITOSIS SPINDLE; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; PROTEIN LOCALIZATION; VERTEBRATE;

ANIMALS; CATTLE; CYTOPLASM; GLYCOSIDE HYDROLASES; HYDROLYSIS; KINESIN; MITOTIC SPINDLE APPARATUS; NUCLEAR PROTEINS; OOCYTES; POLY ADENOSINE DIPHOSPHATE RIBOSE; POLY(ADP-RIBOSE) POLYMERASES; XENOPUS LAEVIS; XENOPUS PROTEINS;

RICKETTSIA SP. PAR; VERTEBRATA;

EID: 10344234720     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03061     Document Type: Article

References (29)

1. Wittmann, T., Hyman, A. & Desai, A. The spindle: a dynamic assembly of microtubules and motors. Nature Cell Biol. 3, E28-E34 (2001).
2. Smith, S. The world according to PARP. Trends Biochem. Sci. 26, 174-179 (2001).
3. Tulin, A., Stewart, D. & Spradling, A. C. The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development. Genes Dev. 16, 2108-2119 (2002).
4. Hatakeyama, K., Nemoto, Y., Ueda, K. & Hayaishi, O. Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose). J. Biol. Chem. 261, 14902-14911 (1986).
5. Saxena, A., Saffery, R., Wong, L. H., Kalitsis, P. & Choo, K. H. Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated. J. Biol. Chem. 277, 26921-26926 (2002).
6. Kickhoefer, V. A. et al. The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase. J. Cell Biol. 146, 917-928 (1999).
7. Smith, S. & de Lange, T. Tankyrase promotes telomere elongation in human cells. Curr. Biol. 10, 1299-1302 (2000).
8. Sbodio, J. I. & Chi, N. W. Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner. J. Biol Chem. 277, 31887-31892 (2002).
9. Bakondi, E. et al. Detection of poly(ADP-ribose) polymerase activation in oxidatively stressed cells and tissues using biotinylated NAD substrate. J. Histochem. Cytochem. 50, 91-98 (2002).
10. Earle, E. et al. Poly(ADP-ribose) polymerase at active centromeres and neocentromeres at metaphase. Hum. Mol. Genet. 9, 187-194 (2000).
11. Smith, S. & de Lange, T. Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes. J. Cell Sci. 112, 3649-3656 (1999).
12. Sawin, K. E. & Mitchison, T. J. Mitotic spindle assembly by two different pathways in vitro. J. Cell Biol. 112, 925-940 (1991).
13. Slama, J. T. et al. Specific inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol. J. Med. Chem. 38, 389-393 (1995).
14. Wilde, A. & Zheng, Y. Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran. Science 284, 1359-1362 (1999).
15. Sawin, K. E., LeGuellec, K., Philippe, M. & Mitchison, T. J. Mitotic spindle organization by a plus-end-directed microtubule motor. Nature 359, 540-543 (1992).
16. Compton, D. A., Szilak, I. & Cleveland, D. W. Primary structure of NuMA, an intranuclear protein that defines a novel pathway for segregation of proteins at mitosis. J. Cell Biol. 116, 1395-1408 (1992).
17. Dionne, M. A., Howard, L. & Compton, D. A. NuMA is a component of an insoluble matrix at mitotic spindle poles. Cell Motil. Cytoskel. 42, 189-203 (1999).
18. Olmsted, J. B., Stemple, D. L., Saxton, W. M., Neighbors, B. W. & McIntosh, J. R. Cell cycle-dependent changes in the dynamics of MAP2 and MAP4 in cultured cells. J. Cell Biol. 109, 211-223 (1989).
19. Kapoor, T. M. & Mitchison, T. J. Eg5 is static in bipolar spindles relative to tubulin: evidence for a static spindle matrix. J. Cell Biol. 154, 1125-1133 (2001).
20. Saxton, W. M. et al. Tubulin dynamics in cultured mammalian cells. J. Cell Biol. 99, 2175-2186 (1984).
21. Wittmann, T., Wilm, M., Karsenti, E. & Vernos, I. TPX2, A novel Xenopus MAP involved in spindle pole organization. J. Cell Biol 149, 1405-1418 (2000).
22. Poirier, G. G., de Murcia, G., Jongstra-Bilen, J., Niedergang, C. & Mandel, P. Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure. Proc. Natl Acad. Sci. USA 79, 3423-3427 (1982).
23. Aoufouchi, S. & Shall, S. Regulation by phosphorylation of Xenopus laevis poly(ADP-ribose) polymerase enzyme activity during oocyte maturation. Biochem. J. 325, 543-551 (1997).
24. Chi, N. W. & Lodish, H. F. Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles. J. Biol. Chem. 275, 38437-38444 (2000).
25. Rouleau, M., Aubin, R. A. & Poirier, G. G. Poly(ADP-ribosyl)ated chromatin domains: access granted. J. Cell Sci. 117, 815-825 (2004).
26. Pickett-Heaps, I. D., Forer, A. & Spurck, T. Traction fibre: toward a "tensegral" model of the spindle. Cell Motil. Cytoskel. 37, 1-6 (1997).
27. Troll, W., Garte, S. & Frenkel, K. Suppression of tumor promotion by inhibitors of poly(ADP)ribose formation. Basic Life Sci. 52, 225-232 (1990).
28. Tirnauer, J. S., Salmon, E. D. & Mitchison, T. J. Microtubule plus-end dynamics in Xenopus egg extract spindles. Mol. Biol. Cell 15, 1776-1784 (2004).
29. Lin, W., Ame, J. C., Aboul-Ela, N., Jacobson, E. L. & Jlacobson, M. K. Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 272, 11895-11901 (1997).