A homotetrameric kinesin-5, KLP61F, bundles microtubules and antagonizes Ncd in motility assays.

A homotetrameric kinesin-5, KLP61F, bundles microtubules and antagonizes Ncd in motility assays. Research Abstract Details 

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A homotetrameric kinesin-5, KLP61F, bundles microtubules and antagonizes Ncd in motility assays. Abstract Text:

Li Tao,Alex Mogilner,Gul Civelekoglu-Scholey,Roy Wollman,James Evans,Henning Stahlberg,Jonathan M Scholey,

BACKGROUND: Mitosis depends upon the cooperative action of multiple microtubule (MT)-based motors. Among these, a kinesin-5, KLP61F, and the kinesin-14, Ncd, are proposed to generate antagonistic-sliding forces that control the spacing of the spindle poles. We tested whether purified KLP61F homotetramers and Ncd homodimers can generate a force balance capable of maintaining a constant spindle length in Drosophila embryos. RESULTS: Using fluorescence microscopy and cryo-EM, we observed that purified full-length, motorless, and tailless KLP61F tetramers (containing a tetramerization domain) and Ncd dimers can all cross-link MTs into bundles in MgATP. In multiple-motor motility assays, KLP61F and Ncd drive plus-end and minus-end MT sliding at 0.04 and 0.1 microm/s, respectively, but the motility of either motor is decreased by increasing the mole fraction of the other. At the "balance point," the mean velocity was zero and MTs paused briefly and then oscillated, taking approximately 0.3 microm excursions at approximately 0.02 microm/s toward the MT plus end and then the minus end. CONCLUSIONS: The results, combined with quantitative analysis, suggest that these motors could act as mutual brakes to modulate the rate of pole-pole separation and could maintain a prometaphase spindle displaying small fluctuations in its steady-state length.

A homotetrameric kinesin-5, KLP61F, bundles microtubules and antagonizes Ncd in motility assays. Publishing Authors By Initials

L Tao,A Mogilner,G Civelekoglu-Scholey,R Wollman,J Evans,H Stahlberg,JM Scholey,

For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

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A homotetrameric kinesin-5, KLP61F, bundles microtubules and antagonizes Ncd in motility assays. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Current biology : CB

VOLUME: 16

Page Numbers: 2293-302

Journal Abbreviation: Curr. Biol.

ISSN: 0960-9822

DAY: 5

MONTH: Dec

YEAR: 2006

A homotetrameric kinesin-5, KLP61F, bundles microtubules and antagonizes Ncd in motility assays. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9107782

A homotetrameric kinesin-5, KLP61F, bundles microtubules and antagonizes Ncd in motility assays. Keywords Mesh Terms:

KEYWORDS: Recombinant Proteins

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: A homotetrameric kinesin-5, KLP61F, bundles microtubules and antagonizes Ncd in motility assays. Information

Substance Name: Kinesin

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for A homotetrameric kinesin-5, KLP61F, bundles microtubules and antagonizes Ncd in motility assays.

AFFILIATION: Laboratory of Cell and Computational Biology, Center for Genetics and Development, University of California, Davis, Davis, California 95616, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM 55507

ACRONYM: GM

MEDLINETA: Curr Biol

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