Eg5 Is Static in Bipolar Spindles Relative to Tubulin: Evidence for a Static Spindle Matrix

We used fluorescent speckle microscopy to probe the dynamics of the mitotic kinesin Eg5 in Xenopus extract spindles, and compared them to microtubule dynamics. We found significant populations of Eg5 that were static over several seconds while microtubules flux towards spindle poles. Eg5 dynamics ar...

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Veröffentlicht in:	The Journal of cell biology 2001-09, Vol.154 (6), p.1125-1133
Hauptverfasser:	Kapoor, Tarun M., Mitchison, Timothy J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - pharmacology Adenylyl Imidodiphosphate - pharmacology Animals Biochemistry Cell biology Cellular biology Chromosomes Cytoplasm - chemistry Dynactin Complex Epithelial cells Humans Imaging Kinesin - drug effects Kinesin - metabolism Kinesin - physiology Kinetics Matrix Microscopy Microscopy, Fluorescence - methods Microtubule-Associated Proteins - pharmacology Microtubules Microtubules - chemistry Microtubules - metabolism Microtubules - physiology Mitosis Mitotic spindle apparatus Molecular Motor Proteins - antagonists & inhibitors Molecular Motor Proteins - metabolism Molecular Motor Proteins - physiology Movement Muscle spindles Pyrimidines - pharmacology Spindle Apparatus - chemistry Spindle Apparatus - metabolism Spindle Apparatus - physiology Thiones - pharmacology Xenopus Xenopus Proteins
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Zusammenfassung:	We used fluorescent speckle microscopy to probe the dynamics of the mitotic kinesin Eg5 in Xenopus extract spindles, and compared them to microtubule dynamics. We found significant populations of Eg5 that were static over several seconds while microtubules flux towards spindle poles. Eg5 dynamics are frozen by adenylimidodiphosphate. Bulk turnover experiments showed that Eg5 can exchange between the spindle and the extract with a half life of
ISSN:	0021-9525 1540-8140
DOI:	10.1083/jcb.200106011