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Probing The Mechanisms Underlying Kinetochore Behavior In Vertebate Cells Using Combinations of Advanced Light and 3-D Electron Microscopy

Published online by Cambridge University Press:  02 July 2020

B. F. McEwen
Affiliation:
Laboratory of Cellular Regulation, Wadsworth Center, NYS Dept. Health, Box 509, Albany, NY12201-0509 Department of Biomédical Sciences, State University of New York, Albany, NY, 12222
A.B. Heagle
Affiliation:
Laboratory of Cellular Regulation, Wadsworth Center, NYS Dept. Health, Box 509, Albany, NY12201-0509
C.L. Rieder
Affiliation:
Laboratory of Cellular Regulation, Wadsworth Center, NYS Dept. Health, Box 509, Albany, NY12201-0509 Department of Biomédical Sciences, State University of New York, Albany, NY, 12222
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Extract

For daughter cells to receive equal copies of the genome during mitosis, the replicated chromosomes must attach to and move bi-directionally on the mitotic spindle. A chromosome becomes attached to the spindle via a pair specialized structures, known as kinetochores, that are positioned on opposite sides of its primary constriction (one on each of the two chromatids). In addition to being the spindle attachment site, kinetochores are also involved in producing and/or transmitting the forces for chromosome motion. In vertebrates the kinetochore closest to a spindle pole at the time of nuclear envelope breakdown usually is the first to attach to the spindle. As a result of this attachment the now “monooriented” chromosome moves toward the closest pole where its only attached kinetochore initiates oscillatory motions toward and away from that pole until the unattached sister kinetochore acquires microtubules (Mts) from the opposite spindle pole.

Type
Innovative Approaches to 3-D Structure/Function Determination for Cells and Organelles
Copyright
Copyright © Microscopy Society of America 1997

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References

1. Skibbens, R. V. et al, J. Cell Biol. 122 (1993) 859.CrossRefGoogle Scholar

2. Rieder, C.L. and Salmon, E.D., J. Cell Biol. 124 (1994) 223.CrossRefGoogle Scholar

3. Hays, T.S. and Salmon, E.D., J. Cell Biol. 110 (1990) 391.CrossRefGoogle Scholar

4. Hyman, A. A. and Mitchison, T.J., Cold Spring Harbor Symp. Quant. Biol. 56 (1991) 745.CrossRefGoogle Scholar

5. Khodjakov, A. and Rieder, C.L., J. Cell Biol. 135(1996) 315.CrossRefGoogle Scholar

6. Mitchison, T.J.,Ann. Rev. Cell Biol. 4 (1988) 527.CrossRefGoogle Scholar

7. McEwen, B.F. et al, J. Cell Biol. (1997) in press.Google Scholar

8. McEwen, B.F. andHeagle, A.B., Int. J. Imaging Syst. Technol 8 (1997) 175.3.0.CO;2-7>CrossRefGoogle Scholar

9. Frank, J. et al, J. Struct. Biol. 116 (1996) 190.CrossRefGoogle Scholar

10. Marko, M. and Leith, A., J. Struct. Biol. 116 (1996) 93.CrossRefGoogle Scholar

11. Khodjakov, H.A. et ai, J. Cell Biol. 136 (1997) 229.CrossRefGoogle Scholar

12. Supported by NSF grants MCB 9420772 and BIR 921904 as well as NIH grants GMS 40198 and NCRR/BTP P41-01219.Google Scholar